protein_name
stringlengths 6
11
| species
stringclasses 299
values | sequence
stringlengths 5
4.97k
| annotation
stringlengths 5
2.1k
⌀ |
|---|---|---|---|
SCRK_SOLTU | Solanum tuberosum | MAVNGSALSSGLIVSFGEMLIDFVPTVSGVSLAEAPGFLKAPGGAPANVAIAVTRLGGKSAFVGKLGDDEFGHMLAGILKTNGVQADGINFDKGARTALAFVTLRADGEREFMFYRNPSADMLLTPDELNLDLIRSAKVFHYGSISLIVEPCRSAHLKAMEVAKEAGALLSYDPNLRLPLWSSEAEARKAIKVSDVELEFLTGSDKIDDESAMSLWHPNLKLLLVTLGEKGCNYYTKKFHGSVGGFHVKTVDTTGAGDSFVGALLTKIVDDQAILEDEARLKEVLRFSCACGAITTTKKGAIPALPTESEALTLLKGGA | May play an important role in maintaining the flux of carbon towards starch formation.
Expressed in swelling stolons and, at higher levels, in developing tubers. Low levels found in leaves and stems from tuberizing plants. |
SECA_SPIOL | Spinacia oleracea | MESCARSASQMSSSSCCRCSSFNQKLKQGGIGGGSLPVSFSCVMIGGGGGRRLIDQERGKVRGRERKIGELMQVRASAQGGLLNLGNLLFNFKGGDPAESTKQQYASTVTLINQLEPQISSLTDSQLTDRTSLLRQRALSGESLDSILPEAFAVVREASKRVLGLRPFDVQLIGGMVLHKGEIAEMRTGEGKTLVAILPAYLNALTGKGVHVVTVNDYLARRDCEWVGQVARFLGLKVGLVQQNMTSEVRRENYLCDITYVTNSELGFDFLRDNLATSVDELVLRGFNFCVIDEVDSILIDEARTPLIISGPAEKPSERYYKAAKIAAAFERDIHYTVDEKQKTVLIMEQGYQDAEEILDVEDLYDPREQWALYILNAIKAKELFLKDVNYIIRGKEILIVDEFTGRVMQGRRWSDGLHQAVEAKEGVPIQNETITLASISYQNFFLQFPKLCGMTGTAATESAEFESIYKLKVTIVPTNKPMIRKDESDVVFRATSGKWRAVVVEISRMHKTGLPVLVGTTSVEQSESLSEQLQQASIPHEVLNAKPENVEREAEIVAQSGRLGAVTIATNMAGRGTDIILGGNAEFMARLKIREMLMPRVVRPGDGGFVSMKKPPPMKTWKVKETLFPCKLSQKNAKLVDEAVQLAVKTWGQRSLSELEAEERLSYSCEKGPAQDEVIAKLRHAFLEVAKEYKTFTDEEKNKVVLAGGLHVIGTERHESRRIDNQLRGRSGRQGDPGSSRFFLSLEDNIFRVFGGDRIQGLMRAFRVEDLPIESKMLTRALDEAQRKVENYFFDIRKQLFEYDEVLNSQRDRVYVERRRALESDNLESLLIEYAELTMDDILEANIGSDAPKENWDLEKLIAKLQQYCYLLNDLTPELLSNNCSTYEDLQDYLRRCGREAYLQKKDMVENQAPGLMKEAERFLILSNIDRLWKEHLQAIKFVQQAVGLRGYAQRDPLIEYKLEGYNLFLEMMAQIRRNVIYSAYQFKPVVVKNQEQQQKGKPDSSNVENKRIGDANLNPVSVTESPSSDSPQNT | Has a central role in coupling the hydrolysis of ATP to the transfer of proteins across the thylakoid membrane.
Subcellular locations: Plastid, Chloroplast stroma, Plastid, Chloroplast thylakoid membrane
A minor fraction is associated with the chloroplast thylakoid membrane. |
SGAT_MAIZE | Zea mays | LDYVYGPGRRAMNSPAVPALTKVLLEDVKKALTNTLSPGDRLLLVDMDEWGVDVALTGSQKALSFPTGMGLVCASPRVFFDWKDYLRTYWHYDQALDLELAVEAWGLSNRYNLSLGLGLNKVAGGKVFRDVGYPVK | Subcellular locations: Peroxisome
Expressed in leaves but not in root tissue or seedlings. |
SGAT_WHEAT | Triticum aestivum | HLFVPGPVNIPDQVLRTLLEDVKKLASRLRSDSQHTIKLLDAYRVFFDWKDYLKKVFRNVNTLLKDLGYPVKPLIPSR | Subcellular locations: Peroxisome
Expressed in leaves but not in root tissue or seedlings. |
SMT1_ORYSJ | Oryza sativa subsp. japonica | MSRSGAMDLASGLGGKITKDEVKSAVDEYEKYHGYYGGKEEARKSNYTDMVNKYYDLATSFYEYGWGESFHFAHRWNGESLRESIKRHEHFLALQLGVKPGMKVLDVGCGIGGPLREIAKFSLASVTGLNNNEYQITRGKELNRVAGVSGTCDFVKADFMKMPFSDNTFDAVYAIEATCHAPDPVGCYKEIYRVLKPGQCFAVYEWCITDHYEPNNATHKRIKDEIELGNGLPDIRSTQQCLQAAKDAGFEVIWDKDLAEDSPVPWYLPLDPSRFSLSSFRLTTVGRAITRTMVKALEYVGLAPQGSERVSNFLEKAAEGLVEGGKKEIFTPMYFFLVRKPISE | Catalyzes the methyl transfer from S-adenosyl-methionine to the C-24 of cycloartenol to form 24-methylene cycloartenol. |
SMT2_ORYSJ | Oryza sativa subsp. japonica | MEAATMAWTAAGVGMALVYWFVWVMGAAEVKGKRAVDLKMGSITNDKVKDKYTQYWSFFRRPKETATTEASAEKVPAFVDTFYNLVTDIYEWGWGQSFHFSPSLPGRSHREATRVHEERVADLLQAKPGHRLLDVGCGVGGPMRAIAAHSGSNVVGITINEYQVNRARAHNRKAGLDSRCEVVCGNFLSMPFSDASFDGAYSIEATCHAPRLQDVYGEVFRVLKPGGLYVSYEWVTTSLYRADNPEHVEAIHGIERGDALPGLRRQDEIASIAKEVGFEVLKELDLALPPALPWWTRLKMGRIAYWRNSLVVRVLTMLRIAPKGVCEVHEMLYETAQHLTRGGETGIFTPMHMVLLRKPVESK | Catalyzes the methyl transfer from S-adenosyl-methionine to the methylene group of 24-methylene lophenol to form 24-ethylidene lophenol.
Subcellular locations: Membrane |
SMTA_ASTBI | Astragalus bisulcatus | MSSPLITDFLHQAGRAAVIAGGLGTELQRHGADLNDPLWSAKCLLSCPHLIRQVHLDYLENGADIIITASYQATIQGFKAKGFSDEEGEALLRRSVEIAREARDLYYQRCAESSSDNGDDSRILKQRPILIAGSVGSYGAYLADGSEFSGNYGDAIKSETLKDFHRRKVQILADSGVDLLAFEAVPNKLEAQAYADLLEEENIITPAWFAFTSKDGNNVVSGDSIEECGSIAESCDKVVAVGINCTPPRFIHDLILLLKKVTAKPIVIYPNSGETYDAIRKEWGQNSGVTDEDFVSYVDKWCESGASLVGGCCRTTPDTIRGIYKILSSGQSPTFSAK | Catalyzes the methylation of selenocysteine with S-methylmethionine as donor. Does not methylate cysteine.
Present in all tissues tested. |
SNP32_ORYSJ | Oryza sativa subsp. japonica | MSGRRSFFASKKPSRSSNPFDSDSDDGGREQRPARASSVPPPADQRGSLFGGGDGFSASSAAARSRYRNDFRDTGGVEAQSVQELEGYAAYKAEETTQRVQGCVRIAEEMRDTASKSLVTIHQQGQQITRTHMMTLDIDQDLSRSEKLLGDLGGIFSKKWKPKKNGEIRGPMLTRDDSFIRKGSHLEQRHKLGLSDHPPQSNARQFHSEPTSALQKVEMEKAKQDDGLSDLSNILTELKGMAVDMGTEIDRQTKALGDSEKDYDELNFRIKGANTRARRLLGK | t-SNARE involved in diverse vesicle trafficking and membrane fusion processes (Probable). May be involved in resistance to the rice blast fungus Magnaporthe oryzae (Ref.6, ). May contribute to host resistance to rice blast through interaction with SYP121 .
Subcellular locations: Membrane
Localizes to the plasma membrane.
Expressed in roots, culms and leaves. |
SODCP_SOLLC | Solanum lycopersicum | MAAHSIFTTTSTTNSFLYPISSSSSSPNINSSFLGVSLNVNAKFGQSLTLYAVTTPKPLTVFAATKKAVAVLKGNSNVEGVVTLSQDDDGPTTVNVRITGLAPGLHGFHLHEYGDTTNGCMSTGAHFNPNKLTHGAPGDEIRHAGDLGNIVANADGVAEVTLVDNQIPLTGPNSVVGRALVVHELEDDLGKGGHELSLTTGNAGGRLACGVVGLTPI | Destroys radicals which are normally produced within the cells and which are toxic to biological systems.
Subcellular locations: Plastid, Chloroplast |
SODCP_SPIOL | Spinacia oleracea | MAAHTILASAPSHTTFSLISPFSSTPTNALSSSLQSSSFNGLSFKLSPTTQSLSLSTSAASKPLTIVAATKKAVAVLKGTSNVEGVVTLTQEDDGPTTVNVRISGLAPGKHGFHLHEFGDTTNGCMSTGPHFNPDKKTHGAPEDEVRHAGDLGNIVANTDGVAEATIVDNQIPLTGPNSVVGRALVVHELEDDLGKGGHELSPTTGNAGGRLACGVVGLTPV | Destroys radicals which are normally produced within the cells and which are toxic to biological systems.
Subcellular locations: Plastid, Chloroplast |
SODC_PEA | Pisum sativum | MVKAVAVLSNSNEVSGTINFSQEGNGPTTVTGTLAGLKPGLHGFHIHALGDTTNGCISTGPHFNPNGKEHGAPEDETRHAGDLGNINVGDDGTVSFTITDNHIPLTGTNSIIGRAVVVHADPDDLGKGGHELSKTTGNAGGRVACGIIGLQG | Destroys radicals which are normally produced within the cells and which are toxic to biological systems.
Subcellular locations: Cytoplasm |
SODM3_MAIZE | Zea mays | MALRTLASKNALSFALGGAARPSAESARGVTTVALPDLSYDFGALEPVISGEIMRLHHQKNHATYVVNYNKALEQIDDVVVKGDDSAVVQLQGAIKFNGGGHVNHSIFWKNLKPISEGGGEPPHGKLGWAIDEDFGSFEALVKRMNAEGAALQGSGWVWLALDKEAKKVSVETTANQDPLVTKGASLVPLLGIDVWEHAYYLQYKNVRPDYLNNIWKVMNWKYAGEVYENVLA | Destroys superoxide anion radicals which are normally produced within the cells and which are toxic to biological systems.
Subcellular locations: Mitochondrion matrix
Predominantly expressed in the embryo late in embryogenesis. |
SODM4_MAIZE | Zea mays | MALRTLASKNALSFALGGAARPSAASARGVTTVALPDLSYDFGALEPAISGEIMRLHHQKHHATYVGNYNKALEQLDAAVAKGDASAVVQLQGAIKFNGGGHVNHSIFWKNLKPISEGGGEPPHGKLGWAIDEDFGSFEALVKRMNAEGAALQGSGWVWLALDKEPKKLSVETTANQDPLVTKGASLVPLLGIDVWEHAYYLQYKNVRPDYLNNIWKVMNWKYAGEVYENVLA | Destroys superoxide anion radicals which are normally produced within the cells and which are toxic to biological systems.
Subcellular locations: Mitochondrion matrix |
SPO11_ORYSI | Oryza sativa subsp. indica | MAGREKRRRVAALDGEERRRRQEEAATLLHRIRGLVRWVVAEVAAGRSPTVALHRYQNYCSSASAAAASPCACSYDVPVGTDVLSLLHRGSHASRLNVLLRVLLVVQQLLQQNKHCSKRDIYYMYPSIFQEQAVVDRAINDICVLFKCSRHNLNVVPVAKGLVMGWIRFLEGEKEVYCVTNVNAAFSIPVSIEAIKDVVSVADYILIVEKETVFQRLANDKFCERNRCIVITGRGYPDIPTRRFLRYLVEQLHLPVYCLVDADPYGFDILATYKFGSLQLAYDANFLRVPDIRWLGVFTSDFEDYRLPDCCLLHLSSEDRRKAEGILSRCYLHREAPQWRLELEAMLQKGVKFEIEALSACSISFLSEEYIPKKIKQGRHI | Required for meiotic recombination. Mediates DNA cleavage that forms the double-strand breaks (DSB) that initiate meiotic recombination (By similarity). May be involved in plant growth and development, and stress tolerance.
Subcellular locations: Nucleus
Highly expressed in flowers before pollination. Expressed in roots and shoots. |
SPO11_ORYSJ | Oryza sativa subsp. japonica | MAGREKRRRVAALDGEERRRRQEEAATLLHRIRGLVRWVVAEVAAGRSPTVALHRYQNYCSSASAAAASPCACSYDVPVGTDVLSLLHRGSHASRLNVLLRVLLVVQQLLQQNKHCSKRDIYYMYPSIFQEQAVVDRAINDICVLFKCSRHNLNVVPVAKGLVMGWIRFLEGEKEVYCVTNVNAAFSIPVSIEAIKDVVSVADYILIVEKETVFQRLANDKFCERNRCIVITGRGYPDIPTRRFLRYLVEQLHLPVYCLVDADPYGFDILATYKFGSLQLAYDANFLRVPDIRWLGVFTSDFEDYRLPDCCLLHLSSEDRRKAEGILSRCYLHREAPQWRLELEAMLQKGVKFEIEALSACSISFLSEEYIPKKIKQGRHI | Required for meiotic recombination. Mediates DNA cleavage that forms the double-strand breaks (DSB) that initiate meiotic recombination. Is essential for both homologous chromosomes pairing and crossover formation during meiosis.
Subcellular locations: Nucleus |
SPO12_ORYSI | Oryza sativa subsp. indica | MAEAGVAAASLFGADRRLCSADILPPAEVRARIEVAVLNFLAALTDPAAPAISALPLISRGAANRGLRRALLRDDVSSVYLSYASCKRSLTRANDAKAFVRVWKVMEMCYKILGEGKLVTLRELFYTLLSESPTYFTCQRHVNQTVQDVVSLLRCTRQSLGIMASSRGALIGRLVLQGPEEEHVDCSILGPSGHAITGDLNVLSKLIFSSDARYIIVVEKDAIFQRLAEDRIYSHLPCILITAKGYPDLATRFILHRLSQTYPNMPIFALVDWNPAGLAILCTYKYGSISMGLESYRYACNVKWLGLRGDDLQLIPQSAYQELKPRDLQIAKSLLSSKFLQDKHRAELTLMLETGKRAEIEALYSHGFDFLGKYVARKIVQGDYI | Required for meiotic recombination. Mediates DNA cleavage that forms the double-strand breaks (DSB) that initiate meiotic recombination (By similarity).
Subcellular locations: Nucleus
Highly expressed in flowers before pollination. Expressed in roots and shoots. |
SPO12_ORYSJ | Oryza sativa subsp. japonica | MAEAGVAAASLFGADRRLCSADILPPAEVRARIEVAVLNFLAALTDPAAPAISALPLISRGAANRGLRRALLRDDVSSVYLSYASCKRSLTRANDAKAFVRVWKVMEMCYKILGEGKLVTLRELFYTLLSESPTYFTCQRHVNQTVQDVVSLLRCTRQSLGIMASSRGALIGRLVVQGPEEEHVDCSILGPSGHAITGDLNVLSKLIFSSDARYIIVVEKDAIFQRLAEDRIYSHLPCILITAKGYPDLATRFILHRLSQTYPNMPIFALVDWNPAGLAILCTYKYGSISMGLESYRYACNVKWLGLRGDDLQLIPQSAYQELKPRDLQIAKSLLSSKFLQDKHRAELTLMLETGKRAEIEALYSHGFDFLGKYVARKIVQGDYI | Required for meiotic recombination. Mediates DNA cleavage that forms the double-strand breaks (DSB) that initiate meiotic recombination (By similarity).
Subcellular locations: Nucleus |
SPO14_ORYSJ | Oryza sativa subsp. japonica | MDDSTDDDSYHPRKHYAYDRQVSSSRWRTSREYIRGPGPETHTTESAQDGQDPPAGVYSYGYFSGSGNDPQVQGHFVPEIQKYNPYVIFKGEQLPVPIWELPEEKVQDFHDRYFIAKDKSRVEARKTLNRLLEGNINTIERGHGYKFNIPKYTDNMEFNEEVKVSLAKAGKTISRSFCNANQREVASRTGYTIDLIERTLGAGLNISKRTVLYTNKDLFGDQSKSDQAINDICALTNIRRGSLGIIAAEKGIVVGNIFLELTNGKSISCSIGVQIPHRLDQIKDVCVEIGSRNIEYILVVEKHTMLNYLLEMDYHTNNNCIILTGCGMPTLQTRDFLRFLKQRTGLPVFGLCDPDPEGISILATYARGSCNSAYDNFNISVPSICWVGLSSSDMIKLNLSETNYSRLSREDKTMLKNLWQDDLSDVWKRRIEEMISFDKKASFEAIHSLGFDYFATNLLPDMINKVREGYVQVQEKKEPQDTEASED | Required for meiotic recombination. Mediates DNA cleavage that forms the double-strand breaks (DSB) that initiate meiotic recombination. Possesses double-stranded DNA cleavage activity in vitro.
Subcellular locations: Nucleus |
SPP_ORYSI | Oryza sativa subsp. indica | MASFPSPPLAAAAAAAPPRLAPGLPLAAAAVRRPSSLARRSSIALAAPANPLRCIHRRAVSPRLRRRTEAVGAASAAIGSLGEEREGCLSCFPRGRRRGRPGLARFAPCALPHTYGLSSLHSGLTGAKIRRRHVLHAAGPDEPHVASPTWSETALDKHYVDQPIGKEELEGFLNTPLPSHPKLVRGQLKNGLRYLILPNKVPANRFEAHMEVHVGSIDEEEDEQGIAHMIEHVAFLGSKKREKLLGTGARSNAYTDFHHTVFHIHSPTKTKEYGEDLLPSVLDALNEIAFHPKFSSSRVEKERRAILSELQMMNTIEYRVDCQLLQHLHSENKLSERFPIGLEEQIHKWDPDKIRRFHERWYYPANATLYLVGEINDIPRAIREIEAVFEHTLPEGEAAPMSTASPFGAMASLFAPKLPGGLAASLTGERSPAADKIKPVKRERQAIRPPVEHKWSLPGVAQDAKPPAIFQHELIQSFSINMFCKIPVNQVQTYKDLRSVLMKRIFLSALHFRINTRYKSSNPPFTSVELDHSDSGREGCTVTTLTVTAEPQNWRSAIKVAVHEVRRLKEFGVTMGEMTRYMDALIKDSEQLAMMIDSVPSVDNLDFIMESDALRHTVMDQLQGHESLLAVAETVTLEEVNTVGAEVLEFISDYGKPDAPLPAAIVACVPKKVHMDGVGETDFEIHPEEITDSIKAGLEEPIYPEPELEVPKELITQSELEDLKLQRKPSFASLSKEENVVKIFDDETGIAQRRLSNGISINYKITQNEARVGVMRLIVGGGRATEDSESKGSVIVGVRTLSEGGCVGNFSREQVELFCVNNLINCSLESNEEFIFMEFRFALRDNGMRAAFQLLHMVLEHNVWLEDAFDRATQLYLSYYRSIPKSLERSTAHKLMLAMLNHDERFVEPSPHSLQKLTLQSVKDAVMNQFVGDNMEVSIVGDFTEEEVESCVLDYLGTVSAPKSSKTQEHIEKISFLPFPSDLHFQQVYIKDTDERACAYIAGPAPNRWGFATEGNDLFNVIRSSSGDAQVSESANTDLTERKHNDVRSHSLFFGITLSLLAEIINSRLFTTVRDSMGLTYDVSFELNLFDKLDLGWYVIAVTSTPSKVHKAVDACKGVLRGLHSNKIVERELDRAKRTLLMKHEAETKTNAYWLGLLAHLQSSSVPRKEISCIKELTMLYESATIEDLYLAYEHLKVDESSLFACIGIAGAESGEETTDDELDMGLHGMGPIGGRGLSTMTRPTT | Cleaves presequences (transit peptides) from chloroplastic protein precursors. Initially recognizes a precursor by binding to the C-terminus of its transit peptide and then removes the transit peptide in a single endoproteolytic step. In a next step, pursues the cleavage of transit peptide to a subfragment form.
Subcellular locations: Plastid, Chloroplast stroma
Widely expressed. |
SPP_ORYSJ | Oryza sativa subsp. japonica | MASFPSPPLAAAAAAAPPRLAPGLPLAAAAVRRPSSLARRSSIALAAPANPLRCIHRRAVSPRLRRRTEAVGAASAAIGSLGEEREGCLSCFPRGRRRGRPGLARFAPCALPHTYGLSSLHSGLTGAKIRRRHVLHAAGPDEPHVASPTWSETALDKHYVDQPIGKEELEGFLNTPLPSHPKLVRGQLKNGLRYLILPNKVPANRFEAHMEVHVGSIDEEEDEQGIAHMIEHVAFLGSKKREKLLGTGARSNAYTDFHHTVFHIHSPTKTKEYGEDLLPSVLDALNEIAFHPKFSSSRVEKERRAILSELQMMNTIEYRVDCQLLQHLHSENKLSERFPIGLEEQIHKWDPDKIRRFHERWYYPANATLYLVGEIDDIPRAIREIEAVFEHTLPEGEAAPMSTASPFGAMASLFAPKLPGGLAASLTGERSPAADKIKPVKRERQAIRPPVEHKWSLPGVAQDAKPPAIFQHELIQSFSINMFCKIPVNQVQTYKDLRSVLMKRIFLSALHFRINTRYKSSNPPFTSVELDHSDSGREGCTVTTLTVTAEPQNWRSAIKVAVHEVRRLKEFGVTMGEMTRYMDALIKDSEQLAMMIDSVPSVDNLDFIMESDALRHTVMDQLQGHESLLAVAETVTLEEVNTVGAEVLEFISDYGKPDAPLPAAIVACVPKKVHMDGVGETDFEIHPEEITDSIKAGLEEPIYPEPELEVPKELITRSELEDLKLQRKPSFASLSKEENVVKIFDDETGIAQRRLSNGISINYKITQNEARVGVMRLIVGGGRATEDSESKGSVIVGVRTLSEGGCVGNFSREQVELFCVNNLINCSLESNEEFIFMEFRFALRDNGMRAAFQLLHMVLEHNVWLEDAFDRATQLYLSYYRSIPKSLERSTAHKLMLAMLNHDERFVEPSPHSLQKLTLQSVKDAVMNQFVGDNMEVSIVGDFTEEEVESCVLDYLGTVSAPKSSKTQEHIEKISFLPFPSDLHFQQVYIKDTDERACAYIAGPAPNRWGFATEGNDLFNVIRSSSGDAQVSESANTDLTERKHNDVRSHSLFFGITLSLLAEIINSRLFTTVRDSMGLTYDVSFELNLFDKLDLGWYVIAVTSTPSKVHKAVDACKGVLRGLHSNKIVERELDRAKRTLLMKHEAETKTNAYWLGLLAHLQSSSVPRKEISCIKELTMLYESATIEDLYLAYEHLKVDESSLFACIGIAGAESGEETTDDELDMGLHGMGPIGGRGLSTMTRPTT | Cleaves presequences (transit peptides) from chloroplastic protein precursors. Initially recognizes a precursor by binding to the C-terminus of its transit peptide and then removes the transit peptide in a single endoproteolytic step. In a next step, pursues the cleavage of transit peptide to a subfragment form.
Subcellular locations: Plastid, Chloroplast stroma |
SPP_PEA | Pisum sativum | MAASTSTSSLSVVGTNLSLPPHRHHRHFHSPSSISTRIRTNRLFLSSSLAFSSPRDARVVHAGLGLRRNTPDVWKHYSSVLSQPTAPVPVRQSCTSCCLASAKKRRSNLPRFVPGAFFDSSSFGLSKDKLRHASVKRVQLPHATVGPDEPHAASTTWQEGVAEKQDLSLFDSELERLEGFLGSELPSHPKLHRGQLKNGIRYLILPNKVPPTRFEAHMEVHVGSIDEEDDEQGIAHMIEHVAFLGSKKREKLLGTGARSNAYTDFHHTVFHIHSPTSTKDSDDLLPSVLDALNEITFHPNFLASRIEKERRAILSELQMMNTIEYRVDCQLLQHLHSENKLSKRFPIGLEEQIKKWDADKIRKFHERWYFPANATLYIVGDIGNIPKTVNQIEAVFGQTGVDNEKGSVATSSAFGAMASFLVPKLSVGLGGNSIERPTNTTDQSKVFKKERHAVRPPVKHTWSLPGSSANLKPPQIFQHELLQNFSINMFCKIPVNKVQTYRDLRIVLMKRIFLSALHFRINTRYKSSNPPFTSVELDHSDSGREGCTVTTLTITAEPKNWQNAIRVAVHEVRRLKEFGVTQGELTRYLDALLRDSEHLAAMIDNVSSVDNLDFIMESDALGHKVMDQSQGHESLIAVAGTVTLDEVNSVGAQVLEFIADFGKLSAPLPAAIVACVPKKVHIEGAGETEFKISSTEITDAMKAGLDEPIEPEPELEVPKELVQSSTLQELKNQRKPAFIPVSPEIEAKKLHDEETGITRLRLANGIPVNYKISKSETQSGVMRLIVGGGRAAEGSDSRGSVIVGVRTLSEGGRVGNFSREQVELFCVNNQINCSLESTEEFISLEFRFTLRNNGMRAAFQLLHMVLEHSVWSDDALDRARQVYLSYYRSIPKSLERSTAHKLMVAMLDGDERFTEPTPSSLENLTLQSVKDAVMNQFVGNNMEVSIVGDFTEEEIESCILDYLGTAQATGNFKNQQQIIPPTFRLSPSSLQSQEVFLNDTDERACAYIAGPAPNRWGFTADGNDLLETIDNASSVNNNGTKSDALQTEGAPRRSLRSHPLFFGITMGLLSEIINSRLFTTVRDSLGLTYDVSFELNLFDRLKLGWYVVSVTSTPSKVHKAVDACKNVLRGLHSNGITVRELDRAKRTLLMRHEAEIKSNAYWLGLLAHLQSSSVPRKDLSCIKDLTSLYEAATIEDTCLAYEQLKVDEDSLYSCIGVSGAQAAQDIAAPVEEEEAGEGYPGVLPMGRGLSTMTRPTT | Cleaves presequences (transit peptides) from chloroplastic protein precursors ( ). Initially recognizes a precursor by binding to the C-terminus of its transit peptide and then removes the transit peptide in a single endoproteolytic step. In a next step, pursues the cleavage of transit peptide to a subfragment form (, ).
Subcellular locations: Plastid, Chloroplast stroma |
SPS2_ORYSJ | Oryza sativa subsp. japonica | MLSVSCPRVYMSRKALDFGQLASCRCRWAGRSGMRVAPRRRMPCVCFVASPSQPGLAAVDVPAEAISSARTTTMIPERISVSSLLEVVSDDLLKLNNNLKSLVGAENPVLVSAAEQIFGAGGKRLRPALVFLVSRATAELAGLLELTTEHQRLAEIIEMIHTASLIHDDVIDDSGMRRGKETIHQLYGTRVAVLAGDFMFAQSSWFLANLENIEVIKLISQVIKDFASGEIKQASTLFDCDVTLDDYLLKSYYKTASLLASSTRSAAIFSGVSTTICEQMYEYGRNLGLSFQVVDDILDFTQSAEQLGKPAGSDLAKGNLTAPVIFALQDEPKLREIIDSEFSESDSLATAIDLVHRSGGIRRAQELAKEKGDLALQNLQCLPKSQFRSTLENVVKYNLQRID | Involved in providing solanesyl diphosphate for plastoquinone-9 (PQ-9) formation. Geranyl diphosphate is the preferred substrate.
Subcellular locations: Plastid, Chloroplast
Expressed in leaves, stems and roots. Highest expression in leaves and roots. |
SPS3_ORYSJ | Oryza sativa subsp. japonica | MAAPSSLASSSHLSRRATAAASPSIPPPSPPPPPQRLRCGWVGRAAPPTRRAPGVCSVVSPSKPGVAAVDVPAATIPDAAATGVGVAERISVSSLLEVVADDLLKLNNNLKSLVGAENPVLVSAAEQIFGAGGKRLRPALVFLVSRATAELAGLLELTTEHQRLAEIIEMIHTASLIHDDVIDDSGMRRGKETIHQLYGTRVAVLAGDFMFAQSSWFLANLENIEVIKLISQVIKDFASGEIKQASTLFDCDITLDDYLLKSYYKTASLIAASTRSAAIFSGVSTAICEQMYEYGRNLGLSFQVVDDILDFTQSAEQLGKPAGSDLAKGNLTAPVIFALQDEPQLREIIDSEFSETNSLATAIELVHRSGGIKRAHELAREKGEIAIQSLQCLPRSEFRSTLENMVKYNLERID | Involved in providing solanesyl diphosphate for plastoquinone-9 (PQ-9) formation.
Subcellular locations: Plastid, Chloroplast |
SPSA1_ORYSI | Oryza sativa subsp. indica | MAGNEWINGYLEAILDSGGAAGGGGGGGGGGGGGGGGGGGGGGGGVDPRSPAAGAASPRGPHMNFNPTHYFVEEVVKGVDESDLHRTWIKVVATRNARERSTRLENMCWRIWHLARKKKQLELEGILRISARRKEQEQVRRETSEDLAEDLFEGEKADTVGELAQQDTPMKKKFQRNFSELTVSWSDENKEKKLYIVLISLHGLVRGDNMELGRDSDTGGQVKYVVELARALAMMPGVYRVDLFTRQVSSPEVDWSYGEPTEMLTSGSTDGEGSGESAGAYIVRIPCGPRDKYLRKEALWPYLQEFVDGALAHILNMSKALGEQVSNGKLVLPYVIHGHYADAGDVAALLSGALNVPMVLTGHSLGRNKLEQIMKQGRMSKEEIDSTYKIMRRIEGEELALDAAELVITSTRQEIDEQWGLYDGFDVKLEKVLRARARRGVSCHGRFMPRMVVIPPGMDFSSVVVPEDTSDGDDGKDFEIASPRSLPPIWAEVMRFLTNPHKPMILALSRPDPKKNITTLVKAFGECRPLRELANLILIMGNRDDIDEMSAGNASVLTTVLKLIDKYDLYGSVAFPKHHKQSDVPEIYRLTGKMKGVFINPALVEPFGLTLIEAAAHGLPIVATKNGGPVDIKNALNNGLLVDPHDQHAIADALLKLVADKNLWQECRKNGLRNIQLYSWPEHCRTYLTRIAGCRIRNPRWLMDTPADAAAEEEEALEDSLMDVQDLSLRLSIDGERGSSMNDAPSSDPQDSVQRIMNKIKRSSPADTDGAKIPAEAAATATSGAMNKYPLLRRRRRLFVIAVDCYGDDGSASKRMLQVIQEVFRAVRSDSQMSRISGFALSTAMPLPETLKLLQLGKIPPTDFDALICGSGSEVYYPSTAQCVDAGGRLRPDQDYLLHINHRWSHDGAKQTIAKLAHDGSGTNVEPDVESCNPHCVSFFIKDPNKVRTIDEMRERVRMRGLRCHLMYCRNATRLQVVPLLASRSQALRYLFVRWGLSVGNMYLIVGEHGDTDHEEMLSGLHKTVIIRGVTEKGSEQLVRSSGSYQREDVVPSESPLIAFTKGDLKADEIMRALKEVTKAASGM | Plays a role in photosynthetic sucrose synthesis by catalyzing the rate-limiting step of sucrose biosynthesis from UDP-glucose and fructose- 6-phosphate. Involved in the regulation of carbon partitioning in the leaves of plants. May regulate the synthesis of sucrose and therefore play a major role as a limiting factor in the export of photoassimilates out of the leaf. Plays a role for sucrose availability that is essential for plant growth and fiber elongation (By similarity).
Expressed in leaves mesophyll cells, scutellum of germinating seedlings and pollen of immature inflorescences. |
SPSA1_ORYSJ | Oryza sativa subsp. japonica | MAGNEWINGYLEAILDSGGAAGGGGGGGGGGGGGGGGGGGGGGGGVDPRSPAAGAASPRGPHMNFNPTHYFVEEVVKGVDESDLHRTWIKVVATRNARERSTRLENMCWRIWHLARKKKQLELEGILRISARRKEQEQVRRETSEDLAEDLFEGEKADTVGELAQQDTPMKKKFQRNFSELTVSWSDENKEKKLYIVLISLHGLVRGDNMELGRDSDTGGQVKYVVELARALAMMPGVYRVDLFTRQVSSPEVDWSYGEPTEMLTSGSTDGEGSGESAGAYIVRIPCGPRDKYLRKEALWPYLQEFVDGALAHILNMSKALGEQVSNGKLVLPYVIHGHYADAGDVAALLSGALNVPMVLTGHSLGRNKLEQIMKQGRMSKEEIDSTYKIMRRIEGEELALDAAELVITSTRQEIDEQWGLYDGFDVKLEKVLRARARRGVSCHGRFMPRMVVIPPGMDFSSVVVPEDTSDGDDGKDFEIASPRSLPPIWAEVMRFLTNPHKPMILALSRPDPKKNITTLVKAFGECRPLRELANLILIMGNRDDIDEMSAGNASVLTTVLKLIDKYDLYGSVAFPKHHKQSDVPEIYRLTGKMKGVFINPALVEPFGLTLIEAAAHGLPIVATKNGGPVDIKNALNNGLLVDPHDQHAIADALLKLVADKNLWQECRKNGLRNIQLYSWPEHCRTYLTRIAGCRIRNPRWLMDTPADAAAEEEEALEDSLMDVQDLSLRLSIDGERGSSMNDAPSSDPQDSVQRIMNKIKRSSPADTDGAKIPAEAAATATSGAMNKYPLLRRRRRLFVIAVDCYGDDGSASKRMLQVIQEVFRAVRSDSQMSRISGFALSTAMPLPETLKLLQLGKIPPTDFDALICGSGSEVYYPSTAQCVDAGGRLRPDQDYLLHINHRWSHDGAKQTIAKLAHDGSGTNVEPDVESCNPHCVSFFIKDPNKVRTIDEMRERVRMRGLRCHLMYCRNATRLQVVPLLASRSQALRYLFVRWGLSVGNMYLIVGEHGDTDHEEMLSGLHKTVIIRGVTEKGSEQLVRSSGSYQREDVVPSESPLIAFTKGDLKADEIMRALKEVTKAASGM | Plays a role in photosynthetic sucrose synthesis by catalyzing the rate-limiting step of sucrose biosynthesis from UDP-glucose and fructose- 6-phosphate. Involved in the regulation of carbon partitioning in the leaves of plants. May regulate the synthesis of sucrose and therefore play a major role as a limiting factor in the export of photoassimilates out of the leaf. Plays a role for sucrose availability that is essential for plant growth and fiber elongation (By similarity).
Expressed in germinating seeds. |
SPSA2_ORYSJ | Oryza sativa subsp. japonica | MAGNDNWINSYLDAILDAGKAAIGGDRPSLLLRERGHFSPARYFVEEVITGYDETDLYKTWLRANAMRSPQERNTRLENMTWRIWNLARKKKEFEKEEACRLLKRQPEAEKLRTDTNADMSEDLFEGEKGEDAGDPSVAYGDSTTGSSPKTSSIDKLYIVLISLHGLVRGENMELGRDSDTGGQVKYVVELAKALSSSPGVYRVDLLTRQILAPNFDRSYGEPTEMLVSTSFKNSKQEKGENSGAYIIRIPFGPKDKYLAKEHLWPFIQEFVDGALGHIVRMSKTIGEEIGCGHPVWPAVIHGHYASAGIAAALLSGSLNIPMAFTGHFLGKDKLEGLLKQGRHSREQINMTYKIMCRIEAEELSLDASEIVIASTRQEIEEQWNLYDGFEVILARKLRARVKRGANCYGRYMPRMVIIPPGVEFGHIIHDFEMDGEEENPCPASEDPPIWSQIMRFFTNPRKPMILAVARPYPEKNITSLVKAFGECRPLRELANLTLIMGNREAISKMNNMSAAVLTSVLTLIDEYDLYGQVAYPKHHKHSEVPDIYRLAARTKGAFVNVAYFEQFGVTLIEAAMNGLPIIATKNGAPVEINQVLNNGLLVDPHDQNAIADALYKLLSDKQLWSRCRENGLKNIHQFSWPEHCKNYLSRILTLGPRSPAIGGKQEQKAPISGRKHIIVISVDSVNKEDLVRIIRNTIEVTRTEKMSGSTGFVLSTSLTISEIRSLLVSAGMLPTVFDAFICNSGSNIYYPLYSGDTPSSSQVTPAIDQNHQAHIEYRWGGEGLRKYLVKWATSVVERKGRIERQIIFEDPEHSSTYCLAFRVVNPNHLPPLKELRKLMRIQSLRCNALYNHSATRLSVVPIHASRSQALRYLCIRWGIELPNVAVLVGESGDSDYEELLGGLHRTVILKGEFNIPANRIHTVRRYPLQDVVALDSSNIIGIEGYSTDDMKSALQQIGVLTQ | Plays a role in photosynthetic sucrose synthesis by catalyzing the rate-limiting step of sucrose biosynthesis from UDP-glucose and fructose- 6-phosphate. Involved in the regulation of carbon partitioning in the leaves of plants. May regulate the synthesis of sucrose and therefore play a major role as a limiting factor in the export of photoassimilates out of the leaf. Plays a role for sucrose availability that is essential for plant growth and fiber elongation (By similarity).
Expressed in germinating seeds. |
SPSA3_ORYSJ | Oryza sativa subsp. japonica | MYGNDNWINSYLDAILDAGKGAAASASASAVGGGGGAGDRPSLLLRERGHFSPARYFVEEVITGYDETDLYKTWLRANAMRSPQEKNTRLENMTWRIWNLARKKKELEKEEANRLLKRRLETERPRVETTSDMSEDLFEGEKGEDAGDPSVAYGDSTTGNTPRISSVDKLYIVLISLHGLVRGENMELGRDSDTGGQVKYVVELAKALSSCPGVYRVDLFTRQILAPNFDRSYGEPVEPLASTSFKNFKQERGENSGAYIIRIPFGPKDKYLAKEHLWPFIQEFVDGALSHIVKMSRAIGEEISCGHPAWPAVIHGHYASAGVAAALLSGALNVPMVFTGHFLGKDKLEELLKQGRQTREQINMTYKIMCRIEAEELALDASEIVIASTRQEIEEQWNLYDGFEVILARKLRARVKRGANCYGRYMPRMVIIPPGVEFGHMIHDFDMDGEEDGPSPASEDPSIWSEIMRFFTNPRKPMILAVARPYPEKNITTLVKAFGECRPLRELANLTLIMGNREAISKMHNMSAAVLTSVLTLIDEYDLYGQVAYPKRHKHSEVPDIYRLAVRTKGAFVNVPYFEQFGVTLIEAAMHGLPVIATKNGAPVEIHQVLDNGLLVDPHDQHAIADALYKLLSEKQLWSKCRENGLKNIHQFSWPEHCKNYLSRISTLGPRHPAFASNEDRIKAPIKGRKHVTVIAVDSVSKEDLIRIVRNSIEAARKENLSGSTGFVLSTSLTIGEIHSLLMSAGMLPTDFDAFICNSGSDLYYPSCTGDTPSNSRVTFALDRSYQSHIEYHWGGEGLRKYLVKWASSVVERRGRIEKQVIFEDPEHSSTYCLAFKVVNPNHLPPLKELQKLMRIQSLRCHALYNHGATRLSVIPIHASRSKALRYLSVRWGIELQNVVVLVGETGDSDYEELFGGLHKTVILKGEFNTSANRIHSVRRYPLQDVVALDSPNIIGIEGYGTDDMRSALKQLDIRAQ | Plays a role in photosynthetic sucrose synthesis by catalyzing the rate-limiting step of sucrose biosynthesis from UDP-glucose and fructose- 6-phosphate. Involved in the regulation of carbon partitioning in the leaves of plants. May regulate the synthesis of sucrose and therefore play a major role as a limiting factor in the export of photoassimilates out of the leaf. Plays a role for sucrose availability that is essential for plant growth and fiber elongation (By similarity).
Expressed in germinating seeds. |
SPY_HORVU | Hordeum vulgare | MESLQGKESNGAVPVCNGGGGAAAPPAKQQLPEGTDALRYANILRSRNKFADALQLYTTVLDKDGANVEALIGKGICLQAQSLPRQALDCFTEAVKVDPKNACALTHCGMIYKDEGHLVEAAEAYQKARSADPSYKAASEFLAIVLTDLGTSLKLAGNTEDGIQKYCEALEVDSHYAPAYYNLGVVYSEMMQFDVALTCYEKAALERPLYAEAYCNMGVIYKNRGELDAAIACYDRCLTISPNFEIAKNNMAIALTDLGTKVKIEGDINQGVAYYKKALFYNWHYADAMYNLGVAYGEMLNFEMAIVFYELALHFNPRCAEACNNLGVIYKDRDNLDKAVECYQMALSIKPNFSQSLNNLGVVYTVQGKMDAAASMIEKAILANPTYAEAYNNLGVLYRDAGSITLSVQAYERCLQIDPDSRNAGQNRLLAMNYIDEGSDDKLYDAHREWGKRFMKLYAQYTSWDNPKVADRPLVIGYVSPDFFTHSVSYFVEAPLTHHDYTKCKVVVYSGVVKADAKTLRFKDKVLKKGGVWRDIYGIDEKKVATLVREDKVDILVELTGHTANNKLGTMACRPAPIQVTWIGYPNTTGLPAIDYRITDSLADSPNTNQKHVEELVRLPESFLCYTPSPEAGPVCPTPAISNGFITFGSFNNLAKITPKVMQVWARILCAVPNSRLVVKCKPFCCDSIRQKFLSTLEELGLESLRVDLLPLIHLNHDHMQAYSLMDISLDTFPYAGTTTTCESLYMGVPCVTMAGSVHAHNVGVSLLTKVGLGRLVAKTEDEYVSLALDLASDVSALEELRKSLRELMIKSPVCDGESFTRGLESAYRSMWHRYCDGDSPALRRLEVLADQTGEDLNKTAVKLADLKAQRVNATAEEDNQSPVTKFDATSKGGEQPQPQIMVNGVTSPEGNQAVKAQPQIMVNGVSSPHSPSGRCEANGHSSR | Probable O-linked N-acetylglucosamine transferase (OGT) involved in various processes such as gibberellin (GA) signaling pathway. OGTs catalyze the addition of nucleotide-activated sugars directly onto the polypeptide through O-glycosidic linkage with the hydroxyl of serine or threonine. Probably acts by adding O-linked sugars to yet unknown proteins.
Subcellular locations: Nucleus
Expressed in all parts of plants, including immature leaf blade, leaf sheath, mature leaf blade, roots, germinating embryos and aleurone layers. |
SPY_ORYSJ | Oryza sativa subsp. japonica | MGRPGMDSSEGRESNGVVPERNGGAVPAKQQLDGKDTLRYANILRSRNKFAEALQLYNNVLEKDEANVEALIGKGICLQAQSLPMQAIECFNEAVRIDPGNACALTYCGMIYKDEGHLVEAAEAYQKARNADPSYKPAAEFLAIVLTDLGTSLKLAGNTEEGIQKYCEALEVDSHYAPAYYNLGVVYSEMMQFDLALTCYEKAALERPLYAEAYCNMGVIYKNRGELEAAIACYERCLTISPNFEIAKNNMAIALTDLGTKVKIEGDINQGVAYYKKALFYNWHYADAMYNLGVAYGEMLNFEMAIVFYELALHFNPRCAEACNNLGVIYKDRDNLDKAVECYQMALSIKPNFSQSLNNLGVVYTVQGKMDAASSMIQKAIFANSTYAEAYNNLGVLYRDAGSITSAVQAYEKCLQIDPDSRNAGQNRLLALNYIDEGFDDKLYQAHREWGKRFLKLYPQYTSWDNPKVADRPLVIGYVSPDYFTHSVSYFIEAPLAHHDYSNYKVVVYSGVVKADAKTLRFKDKVLKKGGLWRDIYGIDEKKVASLVREDKVDILVELTGHTANNKLGTMACRPAPIQVTWIGYPNTTGLPTIDYRITDSLADPPDTTQKHVEELVRLPESFLCYSPSPEAGPVCPTPAILNGFITFGSFNNLAKITPKVLQVWAKILCAVPNSRLVVKCKPFCCDSIRQKFLSTLAELGLEPLRVDLLPLIHLNHDHMQAYSLMDISLDTFPYAGTTTTCESLYMGVPCVTMAGSVHAHNVGVSLLTKVGLGRLVAKSENEYVSLALDLAADVTALQELRMSLRGLMAKSPVCDGENFTRGLESAYRNMWRRYCDGDAPALRRLDLLQEEPCSNNNKQDFDDNQVAKLADLKAQRVDAAVDGDKQSQLTAHAAVVGEVQQAPIMVNGVSSPVSSGKVEANGHISR | Probable O-linked N-acetylglucosamine transferase (OGT) involved in various processes such as gibberellin (GA) signaling pathway. OGTs catalyze the addition of nucleotide-activated sugars directly onto the polypeptide through O-glycosidic linkage with the hydroxyl of serine or threonine. Probably acts by adding O-linked sugars to yet unknown proteins (By similarity).
Subcellular locations: Nucleus |
SPY_SOLLC | Solanum lycopersicum | MAWTEKDVENGKESESLGNNGFLKGGQSSSGSKGSPGRISHVKKIFEDKDAITYANILRSRNKFVDALAIYESVLEKDSKSIESLIGKGICLQMQNTGRLAFESFSEAIKVDPQNACALTHCGILYKDEGRLVEAAESYEKALKADPSYTPAAECLAIVLTDIGTSLKLAGNTQEGIQKYYEAIKIDSHYAPAYYNLGVVYSEMMQYDMALNCYEKAALERPMYAEAYCNMGVIFKNRGDLESAIACYERCLAVSPNFEIAKNNMAIALTDLGTKVKLEGDINQGVAYYKKALCYNWHYADAMYNLGVAYGEMLKFDMAIVFYELAFHFNPHCAEACNNLGVIYKDRDNLDKAVECYQLALSIKPNFSQSLNNLGVVYTVQGKMDAAASMIEKAIIANPTYAEAYNNLGVLYRDAGNISLAIEAYEQCLKIDPDSRNAGQNRLLAMNYINEGTDDKLYEAHRDWGRRFMKLYPQYTSWDNSKVPERPLVIGYVSPDYFTHSVSYFIEAPLAHHDYTNYKVVVYSSVVKADAKTNRFRDKVMKKGGLWRDIYGIDEKKVSSMIREDKVDIMVELTGHTANNKLGTMACRPAPVQVTWIGYPNTTGLPTIDYRITDAMADPPNAKQKHVEELVRLPNSFLCYTPSPEAGPVCPAPALSNGFVTFGSFNNLAKITPKVLKVWARILSAVPHSRLIVKCKPFCCDSVRQRFLSILEQLGLEPQRVDLLPLILLNHDHMQAYSLMDISLDTFPYAGTTTTCESLYMGVPCVTMGGSVHAHNVGVSLLKTVGLENLVARNEDEYVESAIQLASDVTSLSNLRMSLRELMSKSPLCDGAKFTRNIESIYRSMWRRYCDGDVPSLRRMELLQQQQTQTESVVPEESSVNPSERTITSAPTDGSIKENGFTAVPALALKSSTSEENGVQSNHNGNHGNLS | Probable O-linked N-acetylglucosamine transferase (OGT) involved in various processes such as gibberellin (GA) signaling pathway. OGTs catalyze the addition of nucleotide-activated sugars directly onto the polypeptide through O-glycosidic linkage with the hydroxyl of serine or threonine. Probably acts by adding O-linked sugars to yet unknown proteins (By similarity).
Subcellular locations: Nucleus |
SPZ10_ORYSJ | Oryza sativa subsp. japonica | MDYCLQVAWIAGTKAITEQSNFMFSPLGLRAGLALLATGTDGETLRQLLAFLGSQHIHQLNAASAGLLAEMRAWPQLSFAAGIFVDRSLRLRPEFQSTAAAAHGAFPRSVDFQNQANAAAAEVNRFISQATNGRLNNTISPGTFGSSTKCVLANAMHFKATWGRKFESYDTQRRRFHRQDGTRVTVPFLSDPRTHYAARFDGLGFKVLQLFYKMVGHDGQVHFGAPCFCMLVFLPIKRDGLRHLLRMAVTEPDFVMRCVPRSEQEVSPCMVPKFKFSSELDARGALAKLGLGAPFDPLAADLSRMAVSVNTPPERLYVSAMRQKCAVEVDEEGTTAVEATYSCCSPTYSGPESPKPRPMSFVAEHPFMFAIVEYEKAQVLFLGHVMDPSNEE | null |
SPZ11_ORYSJ | Oryza sativa subsp. japonica | MDQCLQVAWIAGSDAITEQSNFIFSPMCLRAGLALLATGADGETLRQMLAFLGSEHIHQLNATSAGLLAEMQAWPQLVFAAGIFVDRSLRLRPEFKSTAAAAHGGIHAICGLPEPDHEGALNQRHPPWHLEQRHDVRPCERHALQGEVGSDVRVVEHHAGNVPPPRRHDGAGAVPVGPRDALRRQGAKFEFHGLEFKVLQLFYKMVGRDGQVDFGFGAPCFCMLVFLPIKRDGLRHLLRMAVTEPDFVTRCVPRSRQIVTPCKVPKFKFSSQLDAGGALAQLGLGAPFDPDAADLSRMAVNTPPAGLYVSTMRQKCAVEVDEEGTTAVEAMYSPSSPGYSPGYQPPRPPPMSFVAEHPFMFAIVEYKKAQVLFLGHVMDPSKEDQ | null |
SPZ12_ORYSJ | Oryza sativa subsp. japonica | MAALAAGEPFSGRATGGDGGVRSDVMAPPAMAEEAKVSCLPLAREVGRRAAAAGGGQGRNFIVSPLSFHAALALVADGARGETQRELLGFLGSPSLAELHRSPTTRLVARLRHLPNTSFACGVWVDRGRALTPEFADAAASRYAAVAEPADFATQPEQARERVNAFVSDATEGLIRDVLPPNSVDSSTVVVLANAVHFKGTWSLPFHPSATFHAPFHLLDGGAVRAPFMTTEIPFERHVAAFPGFTALKLPYKNVGGGGGGDGVPRAAFYMLLLLPDGDGALKLADLYDMAVTTPEFIKKHTPAAEAPVRRLMVPKFKFSFKFEAKSDMRKLGVTRAFAGGDFSGMVTGGDGLFIAEVYHQATIEVDELGTVAAASTAVVMMQKGSSLPPVDFVADRPFLFAVVEELTGAVLFLGHVVNPLAE | Probable serine protease inhibitor. |
SPZ1A_WHEAT | Triticum aestivum | MATTLATDVRLSIAHQTRFALRLASTISSNPKSAASNAAFSPVSLYSALSLLAAGAGSATRDQLVATLGTGKVEGLHALAEQVVQFVLADASSTGGSACRFANGVFVDASLLLKPSFQEIAVCKYKAETQSVDFQTKAAEVTTQVNSWVEKVTSGRIKDILPPGSIDNTTKLVLANALYFKGAWTEQFDSYGTKNDYFYLLDGSSVQTPFMSSMDDQYLLSSDGLKVLKLPYKQGGDNRQFFMYILLPEAPGGLSSLAEKLSAEPDFLERHIPRQRVALRQFKLPKFKISFGIEASDLLKCLGLQLPFGDEADFSEMVDSLMPQGLRVSSVFHQAFVEVNEQGTEAAASTAIKMVLQQARPPSVMDFIADHPFLFLVREDISGVVLFMGHVVNPLLSS | Inhibits chymotrypsin and cathepsin G in vitro. |
SPZ1B_WHEAT | Triticum aestivum | MATTLATDVRLSIAHQTRFALRLASTISSNPKSAASNAAFSPVSLHSALSLLAAGAGSATRDQLVATLGTGEVEGGHALAEQVVQFVLADASSAGGPRVAFANGVFVDASLLLKPSFQELAVCKYKAETQSVDFQTKAAEVTTQVNSWVEKVTSGRIKNILPSGSVDNTTKLVLANALYFKGAWTDQFDSYGTKNDYFYLLDGSSVQTPFMSSMDDDQYISSSDGLKVLKLPYKQGGDNRQFSMYILLPEAPGGLSSLAEKLSAEPDFLERHIPRQRVAIRQFKLPKFKISFGMEASDLLKCLGLQLPFSDEADFSEMVDSPMPQGLRVSSVFHQAFVEVNEQGTEAAASTAIKMVPQQARPPSVMDFIADHPFLFLLREDISGVVLFMGHVVNPLLSS | Inhibits chymotrypsin and cathepsin G in vitro. |
SPZ1C_WHEAT | Triticum aestivum | MATTLATDVRLSIAHQTRFALRLASTISSNPKSAASNAVFSPVSLHVALSLLAAGAGSATRDQLVATLGTGEVEGLHALAEQVVQFVLADASSAGGPHVAFANGVFVDASLPLKPSFQELAVCKYKADTQSVDFQTKAAEVATQVNSWVEKVTSGRIKDILPSGSVDNTTKLVLANALYFKGAWTDQFDSSGTKNDYFYLPDGSSVQTPFMSSMDDQYLSSSDGLKVLKLPYKQGGDKRQFSMYILLPEAPGGLSNLAEKLSAEPDFLERHIPRQRVALRQFKLPKFKISFETEASDLLKCLGLQLPFSNEADFSEMVDSPMAHGLRVSSVFHQAFVEVNEQGTEAAASTAIKMALLQARPPSVMDFIADHPFLFLLREDISGVVLFMGHVVNPLLSS | Inhibits chymotrypsin and cathepsin G in vitro. |
SPZ1_ORYSJ | Oryza sativa subsp. japonica | MELAEAVRDETAMAMRLLGHLARAPRGGGGDKNLAVSPLSLHAALALLGAGARGETLDQIIAFLGPAGGPAHAALASHVALCSLADDSGPGDDRGGPKVRFANGVWVDAALRLKAAYARVVADKYRAEARPVSFRDKLEEARREINEWFESATAGRIKDFLPKDAVDRATPAVLGNALYFKGDWESKFDARSTSDDVFYLPDGGHVSAPFMSSGKWQYIACRAGYKVLRLPYARGGRGRGRDTGRLFSMYIYLPDERHGLPDMLRKLCSDPAALIESSAALTEKVPVGAFMVPRFTLSYKTNAAETLRQLGLRLPFEYPGADLSEMVESSPEAEKIVVSAVYHESFVEVNEEGTEAAAATAVVMTLGCAAPSAPVHVVDFVADHPFMFLIKEDLTGVVVFAGQVTNPSSST | Probable serine protease inhibitor. |
SPZ2A_ORYSJ | Oryza sativa subsp. japonica | MEDNAGDCGGMTAFALRLAKRLADVGVSSNKNLVFSPASLYAALALVAAGARGTTLDELLALLGAASLDDLEESVRRAVEVGLADESASGGPRVSDACGVWHDETLELKPAYRAAAAGTYKAVTRAANFQRQPKRSRKKINKWVSKATNKLIPEILPDGSVHVDTALVLVNAIYFKGKWSNPFPRSSTTTGKFHRLDGSSVDVPFMSSREDQYIGFHDGFTVLKLPYHHRTMKNHGDGGDTITNSSITRAILEHYGGENVGLSMYIFLPDERDGLPALVDKMAASSSSSSFLRDHRPTRRREVGDLRVPRFKVSFYSQINGVLQGMGVTAAFDAGEADLSGMAEGVDQRGGGLVVEEVFHRAVVEVNEEGTEAAASTACTIRLLSMSYPEDFVADHPFAFFVVEETSGAVLFAGHVLDPTSSSE | Probable serine protease inhibitor. |
SSRP1_VICFA | Vicia faba | MTDGHLFNNITLGXRGGTNPGQIKIYSGGILWKRQGGGKTIDVDKTDIMGVTWMKVPKTNQLGVQIKDGLLYKFTGFRDQDVVSLTNFFQNTFGITVEEKQLSVTGRNWGEVDLNGNMLAFMVGSKQAFEVSLADVSQTNLQGKNDVILEFHVDDTTGANEKDSLMEMSFHIPSSNTQFVGDENRPSAQVFRDKIMSMADVGVGGEDAVVTFDGIAILTPRGRYSVELHLSFLRLQGQANDFKIQYSSVVRLFLLPKSNQPHTFVIISLDPPIRKGQTLYPHIVMQFETDTVVDSELAISEDLYNSKYKDKLELSYKGLIHEVFTTVLRGLSGGKVTKPGNFRSCQDGYAVKSSLKAEDGILYPLEKSFFFLPKPPTLILHEEIDYVEFERHAAGGSNMHYFDLLIRLKSEQEHLFRNIQRNEYHNLYGFISSKGLKIMNIADAQQAVGGVAKVLENDDDDAVDPHLERIRNEAGGDESDEEDSDFVIDKDDGGSPTDDSGADVSDASQSGGETEKPAKKEPKKDLSSKASSSKKKSKDADVDGVKKKQKKKKDPNAPKRALSGFMFFSQMERENLKKTNPGISFTDVGRVLGEKWKNLSAEEKEPYEAKAQADKKRYKDEISGYKNPQPMNVDSGNESDSA | Component of the FACT complex, a general chromatin factor that acts to reorganize nucleosomes. The FACT complex is involved in multiple processes that require DNA as a template such as mRNA elongation, DNA replication and DNA repair. During transcription elongation the FACT complex acts as a histone chaperone that both destabilizes and restores nucleosomal structure. It facilitates the passage of RNA polymerase II and transcription by promoting the dissociation of one histone H2A-H2B dimer from the nucleosome, then subsequently promotes the reestablishment of the nucleosome following the passage of RNA polymerase II. Binds specifically to double-stranded DNA (By similarity).
Subcellular locations: Nucleus, Chromosome |
STAD2_ORYSI | Oryza sativa subsp. indica | MALRPNDVTLRLTPPLAAAARRNRRAAAGGVRVYAVASGAVSTKVENKKPFAPPREVHVQVTHSMPPQKIEIFKSLDDWARDNILSHLKPVEKCWQPQDFLPDPASDGFHDEVKELRERAKEIPDDYFVCLVGDMITEEALPTYQTMLNTLDGVRDETGASPTAWAVWTRAWTAEENRHGDLLNKYLYLTGRVDMRQIEKTIQYLIGSGMDPRTENNPYLGFIYTSFQERATFISHGNTARHAKDFGDLKLAQICGIIASDEKRHETAYTKIVEKLFEIDPDGTVLAFADMMKKKISMPAHLMFDGEDDKLFEHFSMVAQRLGVYTAKDYADILEFLVSRWKISDLTGLSSEGNKAQDYLCTLAARIRRLDERAQSRAKKAGTLPFSWVYGREVQL | Converts stearoyl-ACP to oleoyl-ACP by introduction of a cis double bond between carbons 9 and 10 of the acyl chain. Required for the repression of the salicylic acid (SA) signaling pathway.
Subcellular locations: Plastid, Chloroplast |
STAD2_ORYSJ | Oryza sativa subsp. japonica | MALRPNDVTLRLTPPLAAAARRNRRAAAGGVRVYAVASGAVSTKVENKKPFAPPREVHVQVTHSMPPQKIEIFKSLDDWARDNILSHLKPVEKCWQPQDFLPDPASDGFHDEVKELRERAKEIPDDYFVCLVGDMITEEALPTYQTMLNTLDGVRDETGASPTAWAVWTRAWTAEENRHGDLLNKYLYLTGRVDMRQIEKTIQYLIGSGMDPRTENNPYLGFIYTSFQERATFISHGNTARHAKDFGDLKLAQICGIIASDEKRHETAYTKIVEKLFEIDPDGTVLAFADMMKKKISMPAHLMFDGEDDKLFEHFSMVAQRLGVYTAKDYADILEFLVSRWKISDLTGLSSEGNKAQDYLCTLAARIRRLDERAQSRAKKAGTLPFSWVYGREVQL | Converts stearoyl-ACP to oleoyl-ACP by introduction of a cis double bond between carbons 9 and 10 of the acyl chain. Required for the repression of the salicylic acid (SA) signaling pathway.
Subcellular locations: Plastid, Chloroplast |
STAD3_ORYSI | Oryza sativa subsp. indica | MSLTGCLPPRPPCSMRRRTSGGGASVSPVVVMASTAGVGGIGNPTPRGKKPFAPWREVPPQVTHTLPPEKKEVFDSLEGWAADTILPYLKPVEESWQPQDHLPDPRSPSFGDEVAALRERAAGLPDDHLVCLVGDMVTEEALPTYQTMLNTMDGGVRDETGAGGSAWAVWTRAWAAEENRHGDLMNKYLYLTGRVDMRQVEKTIQYLIGSGMDPRTENDPYMGFIYTTFQERATSISHGNTARHAGRHGDAALARVCGTVAADEKRHEAAYAAIVAKLFEVDPDYTVRAFARMMRRKVAMPARLMYDGADDRLFARFAAVAQRLGVYTAADYAGIIEFLVARWGVPGLAAGLSGEGRRAQDFVCSLGPRFRRMEERAQEAAKRAPPAAAAPFSWIHGRQVQL | Introduces a cis double bond in the acyl chain of an acyl-[acyl-carrier protein].
Subcellular locations: Plastid, Chloroplast |
STAD3_ORYSJ | Oryza sativa subsp. japonica | MSLTGCLPPRPPCSMRRRTSGGGASVSPVVAMASTAGVGGIGNPTPRGKKPFAPWREVPPQVTHTLPPEKKEVFDSLEGWAADTILPYLKPVEESWQPQDHLPDPRSPSFGDEVAALRERAAGLPDDHLVCLVGDMVTEEALPTYQTMLNTMDGGVRDETGAGGSAWAVWTRAWAAEENRHGDLMNKYLYLTGRVDMRQVEKTIQYLIGSGMDPRTENDPYMGFIYTTFQERATSISHGNTARHAGRHGDAALARVCGTVAADEKRHEAAYAAIVAKLFEVDPDYTVRAFARMMRRKVAMPARLMYDGADDRLFARFAAVAQRLGVYTAADYAGIIEFLVARWGVPGLAAGLSGEGRRAQDFVCSLGPRFRRMEERAQEAAKRAPPAAAAPFSWIHGRQVQL | Introduces a cis double bond in the acyl chain of an acyl-[acyl-carrier protein].
Subcellular locations: Plastid, Chloroplast |
STAD4_ORYSJ | Oryza sativa subsp. japonica | MASSGLAVAATASSAWLCCPNHHIHTSSSRSRKHLLLHGLYGSAPARTRGRRPPVWTAAAATAAAPADTAASARREQVEIARSLNAWVEENMLPLLTPVDSAWQPHDFLPCSAAGGGEALAAFTEGVAELRAGAAGVPDEVLVCLVGNMVTEEALPTYQSMGNRAEGLADGTGVSPLPWARWLRGWTAEENRHGDLLNRYLYLSGRVDMRQVEATVHRLLRNGMEMLAPASPYHGLIYGAFQERATFISHGHTARLAGQHGDRALAKICGVIAADERRHEAGYTMASGRLFELDPDGMARALADVMRGKVTMPGQLMSDGRDGDGEHSLFARFSAVAERAGVYTARDYGDLVEHFVRRWRVAELAAGLSGEGRRAQEYLCGLAPKIRRMEELAHRRAARIEPAMARFSWIFDRPVMLG | Introduces a cis double bond in the acyl chain of an acyl-[acyl-carrier protein].
Subcellular locations: Plastid, Chloroplast |
STAD5_ORYSI | Oryza sativa subsp. indica | MAFAPSHTASPSYCGVAQGGRRSNGMSPVVAMASTINRVKTAKKPYTPPREVHLQVKHSLPPQKREIFDSLQPWAKENLLNLLKPVEKSWQPQDFLPDPSSDGFYDEVKELRERAKEIPDDYFVCLVGDMVTEEALPTYQTMLNTLDGVRDETGASPTTWAVWTRAWTAEENRHGDLLNKYMYLTGRVDMKQIEKTIQYLIGSGMDPGTENNPYLGFLYTSFQERATFISHGNTARHAKEYGDLKLAQICGTIAADEKRHETAYTKIVEKLFEIDPDYTVLAFADMMRKKISMPAHLMYDGKDDNLFEHFSAVAQRLGVYTARDYADILEFLVQRWKVADLTGLSGEGRRAQDFVCTLAPRIRRLDERAQARAKQAPVIPFSWVYDRKVQL | Converts stearoyl-ACP to oleoyl-ACP by introduction of a cis double bond between carbons 9 and 10 of the acyl chain.
Subcellular locations: Plastid, Chloroplast |
STAD5_ORYSJ | Oryza sativa subsp. japonica | MAFAASHTASPSSCGGVAQRRSNGMSPVVAMASTINRVKTAKKPYTPPREVHLQVKHSLPPQKREIFDSLQPWAKENLLNLLKPVEKSWQPQDFLPDPSSDGFYDEVKELRERAKEIPDDYFVCLVGDMVTEEALPTYQTMLNTLDGVRDETGASPTTWAVWTRAWTAEENRHGDLLNKYMYLTGRVDMKQIEKTIQYLIGSGMDPGTENNPYLGFLYTSFQERATFISHGNTARHAKEYGDLKLAQICGTIAADEKRHETAYTKIVEKLFEIDPDYTVLAFADMMRKKISMPAHLMYDGKDDNLFEHFSAVAQRLGVYTARDYADILEFLVQRWKVADLTGLSGEGRRAQDFVCTLAPRIRRLDERAQARAKQAPVIPFSWVYDRKVQL | Converts stearoyl-ACP to oleoyl-ACP by introduction of a cis double bond between carbons 9 and 10 of the acyl chain.
Subcellular locations: Plastid, Chloroplast, Plastid
In green tissue, found in chloroplasts. In non-photosynthetic tissue, found in plastids. |
STAD6_ORYSI | Oryza sativa subsp. indica | MAATATMAMPLANRLRCKPNTNSSSPSRTLFGRRVTMISSSRWMCRGSAVSGSAIMSAAADDVAAVRREEDEEMRSYLSPEKLEVLTQMEPWVEEHVLPLLKPVEAAWQPSDLLPDPAVLGGEGFHAACAELRERAAGVPDLLLVCLVANMVTEEALPTYQSSLNRVRAVGDLTGADATAWARWIRGWSAEENRHGDVLNRYMYLSGRFDMAEVERAVHRLIRSGMAVDPPCSPYHAFVYTAFQERATAVAHGNTARLVGARGHGDAALARVCGTVAADEKRHEAAYTRIVSRLLEADPDAGVRAVARMLRRGVAMPTSPISDGRRDDLYACVVSLAEQAGTYTVSDYCSIVEHLVWEWRVEELAAGLSGEGRRARDYVCELPQKIRRMKEKAHERAVKAQKKPISIPINWIFDRHVSVMLP | Introduces a cis double bond in the acyl chain of an acyl-[acyl-carrier protein].
Subcellular locations: Plastid, Chloroplast |
STAD6_ORYSJ | Oryza sativa subsp. japonica | MAATATMAMPLANRLRCKPNTNSSSPSRTLFGRRVTMISSSRWGSAVSGSAIMSAAADVAAAVRREEDEEMRSYLSPEKLEVLTQMEPWVEEHVLPLLKPVEAAWQPSDLLPDPAVLGGEGFHAACAELRERAAGVPDLLLVCLVANMVTEEALPTYQSSLNRVRAVGDLTGADATAWARWIRGWSAEENRHGDVLNRYMYLSGRFDMAEVERAVHRLIRSGMAVDPPCSPYHAFVYTAFQERATAVAHGNTARLVGARGHGDAALARVCGTVAADEKRHEAAYTRIVSRLLEADPDAGVRAVARMLRRGVAMPTSPISDGRRDDLYACVVSLAEQAGTYTVSDYCSIVEHLVREWRVEELAAGLSGEGRRARDYVCELPQKIRRMKEKAHERAVKAQKKPISIPINWIFDRHVSVMLP | Introduces a cis double bond in the acyl chain of an acyl-[acyl-carrier protein].
Subcellular locations: Plastid, Chloroplast |
STAD7_ORYSI | Oryza sativa subsp. indica | MAASATTSTLAVTMFGYPNRNCHLKPPATATLRFWRSAAAAAVATSRREAEAEEADEVRRCLAPARLEVLEQMEPWVEAHVLPLLKPAEEAWQPADLVPDAAALGADGFHAACVELRGRAAGVPDAHLVCLVGNMVTEEALPTYQSMANRFESARDVTGADATAWARWIRGWSAEENRHGDVLNRYMYLSGRLDMRQVERTVHRLIGSGMAMHAPASPYHGFIYVAFQERATAISHGNTARNVRAHGDDALARICGAIASDEKRHEAAYTRVVERLLEADPDTTVRALAYMMRRRITMPAALMDDGRDADLFAHYAAAAQQAGTYTASDYRGILEHLIRRWRVAELEAGLSGEGRRARDYVCALPQKIRRMEEKAHDRAAQMRKRPTAIPFSWIFDKPVDLMLP | Introduces a cis double bond in the acyl chain of an acyl-[acyl-carrier protein].
Subcellular locations: Plastid, Chloroplast |
STAD7_ORYSJ | Oryza sativa subsp. japonica | MAASATTSTLAVTMFGYPNRNCHLKPPATATLRFWRSAAAAAVATSRREAEAEEADEVRRCLAPARLEVLEQMEPWVEAHVLPLLKPAEEAWQPADLVPDAAALGADGFHAACVELRGRAAGVPDAHLVCLVGNMVTEEALPTYQSMANRFESARDVTGADATAWARWIRGWSAEENRHGDVLNRYMYLSGRLDMRQVERTVHRLIGSGMAMHAPASPYHGFIYVAFQERATAISHGNTARNVRAHGDDALARICGAIASDEKRHEAAYTRVVERLLEADPDTTVRALAYMMRRRITMPAALMDDGRDADLFAHYAAAAQQAGTYTASDYRGILEHLIRRWRVAELEAGLSGEGRRARDYVCALPQKIRRMEEKAHDRAAQMRKRPTAIPFSWIFDKPVDLMLP | Introduces a cis double bond in the acyl chain of an acyl-[acyl-carrier protein].
Subcellular locations: Plastid, Chloroplast |
SUMO1_ORYSJ | Oryza sativa subsp. japonica | MSAAGEEDKKPAGGEGGGAHINLKVKGQDGNEVFFRIKRSTQLKKLMNAYCDRQSVDMNAIAFLFDGRRLRGEQTPDELEMEDGDEIDAMLHQTGGCLPA | Ubiquitin-like protein which can be covalently attached to target lysines as a monomer. Does not seem to be involved in protein degradation and may function as an antagonist of ubiquitin in the degradation process (By similarity).
Subcellular locations: Nucleus, Cytoplasm |
SUV3L_ORYSI | Oryza sativa subsp. indica | MAAAAAIAAALLRRSTSSQHHRRILLLPLLSHLQRAAPRSPSPWDPPPHHRFFFSSDVTAEGDSKPRPPLDGKQLWREVSTSEPATGASRLPKATWDAVVALLRRFGKDPAMSDQALALYIPASAFPTYARRFRHFLPARLSLESAEHLLSLPADDAHALLLPAFAEFCVTHLADELRKHESVMAAADLTAPHAWYPFARAMRRRVVYHCGPTNSGKTHNALTRFAAAKSGVYCSPLRLLAMEVFDKVNALGVYCSLRTGQEIKEVPFSNHVACTIEMLSTEEPYEVAVVDEIQMMADPVRGYAWTRAVLGLKADEIHLCGDPSVLKIVRKICADTGDDLEVHQYERFKPLVVEAKTLLGDLKNVRSGDCIVAFSRREIFEVKLAIEKFTKHKCCVIYGALPPETRRQQAKLFNEQDNEYDVLVASDAVGMGLNLNIRRVVFYSLAKYNGDRMVPVAASQVKQIAGRAGRRGSIYPDGLTTTFLLDDLDYLIQCLQQPFEEAKKVGLFPCFEQVESFAIQFPDLTFNELLDKFRENCRVDSTYFMCHQESIKKVANMLERIQGLSLKDRYNFCFAPVNIRDPKAMYHLLRFATNYSQSRRVSIAMGMPKGSAKNDTELLDLETKHQVLSMYLWLSHHFEEDHFPHVQKAEEMSINIADLLAKSLAKASWKPTSRQQAKPRRENEEDNDVEQASDDNAKNDSEDGYERSISRIKPFMRKRLDRPSQDPSSLNFVA | Major helicase player in mitochondrial RNA metabolism. Component of the mitochondrial degradosome (mtEXO) complex, that degrades 3' overhang double-stranded RNA with a 3'-to-5' directionality in an ATP-dependent manner. ATPase and ATP-dependent multisubstrate helicase, able to unwind double-stranded (ds) DNA and RNA, and RNA/DNA heteroduplexes in the 5'-to-3' direction. Plays a role in the RNA surveillance system in mitochondria; regulates the stability of mature mRNAs, the removal of aberrantly formed mRNAs and the rapid degradation of non coding processing intermediates (By similarity).
Subcellular locations: Nucleus, Mitochondrion matrix, Mitochondrion matrix, Mitochondrion nucleoid |
SUV3L_ORYSJ | Oryza sativa subsp. japonica | MAAAAAIAAALLRRSTSSQHHRRILLLPLLSHLQRAAPRSPSPWDPPPHHRFFFSSDVTAEGDSKPRPPLDGKQLWREVSTSEPATGASRLPKATWDAVVALLRRFGKDPAMSDQALALYIPASAFPTYARRFRHFLPARLSLESAEHLLSLPADDAHALLLPAFAEFCVTHLADELRKHESVMAAADLTAPHAWYPFARAMRRRVVYHCGPTNSGKTHNALTRFAAAKSGVYCSPLRLLAMEVFDKVNALGVYCSLRTGQEIKEVPFSNHVACTIEMLSTEEPYEVAVVDEIQMMADPVRGYAWTRAVLGLKADEIHLCGDPSVLKIVRKICADTGDDLEVHQYERFKPLVVEAKTLLGDLKNVRSGDCIVAFSRREIFEVKLAIEKFTKHKCCVIYGALPPETRRQQAKLFNEQDNEYDVLVASDAVGMGLNLNIRRVVFYSLAKYNGDRMVPVAASQVKQIAGRAGRRGSIYPDGLTTTFLLDDLDYLIQCLQQPFEEAKKVGLFPCFEQVESFAIQFPDLTFNELLDKFRENCRVDSTYFMCHQESIKKVANMLERIQGLSLKDRYNFCFAPVNIRDPKAMYHLLRFATNYSQSRRVSIAMGMPKGSAKNDTELLDLETKHQVLSMYLWLSHHFEEDHFPHVQKAEEMSINIADLLAKSLAKASWKPTSRQQAKPRRENEEDNDVEQASDDNAKNDSEDGYERSISRIKPFMRKRLDRPSQDPSSLNFVA | Major helicase player in mitochondrial RNA metabolism. Component of the mitochondrial degradosome (mtEXO) complex, that degrades 3' overhang double-stranded RNA with a 3'-to-5' directionality in an ATP-dependent manner. ATPase and ATP-dependent multisubstrate helicase, able to unwind double-stranded (ds) DNA and RNA, and RNA/DNA heteroduplexes in the 5'-to-3' direction. Plays a role in the RNA surveillance system in mitochondria; regulates the stability of mature mRNAs, the removal of aberrantly formed mRNAs and the rapid degradation of non coding processing intermediates (By similarity). Confers salinity and drought stress tolerances by maintaining both photosynthesis and antioxidant machinery, probably via an increase in plant hormones levels such as gibberellic acid (GA(3)), the cytokinin zeatin (Z) and indole-3-acetic acid (IAA) (By similarity).
Subcellular locations: Nucleus, Mitochondrion matrix, Mitochondrion matrix, Mitochondrion nucleoid |
SUV3M_ORYSJ | Oryza sativa subsp. japonica | MAVAAALLRRRALYSALASPSWLHDTSSCYICSISGTHSLVNHPNLRLQRGYHNSGKFDLTDLTHPHIWYPNAREKKRNVFLHVGPTNSGKTHNALKRLEASSSGVYCGPLRLLAREVAQRLNKANVPCNLITGQEREEIEGAKHSSVTVEMADMTTEYQCAVIDEIQMVGCRSRGFSFTRALLGLCSDELHVCGDPAVVPLIQRILEPTGDVVTVQYYERLSPLVPLKTTLGSFSNIKAGDCVVTFSRRSIYMLKRRIEMGGKHLCSVVYGSLPPETRTKQATMFNDQDSNLNVLVASDAIGMGLNLNISRIIFSTLEKFDGICNRELTVAEIKQIAGRAGRYGSKFPVGEVTCLNSDHLPLLHSALKSPSPIIERAGLFPTFDVLSLYSRLHGTDFFQPILERFLDKAKLSPDYFIADCEDMLKVAAIVDELPLGLYDKYLFCLSPVDIRDDISTKGLIQFAENYAKKGIVRLKEIFTPGTLQVPKSHNQLKELESIHKVLELYVWLSFRLEDSYPDRELAASQKSICSMLIEEYLERSGWQQNGRKDFLQKPKRLHQEYDASQLRKYFQEIDVRSK | Major helicase player in mitochondrial RNA metabolism. Component of the mitochondrial degradosome (mtEXO) complex, that degrades 3' overhang double-stranded RNA with a 3'-to-5' directionality in an ATP-dependent manner (By similarity). ATPase and ATP-dependent multisubstrate helicase, able to unwind double-stranded (ds) DNA and RNA, and RNA/DNA heteroduplexes in the 5'-to-3' direction . Plays a role in the RNA surveillance system in mitochondria; regulates the stability of mature mRNAs, the removal of aberrantly formed mRNAs and the rapid degradation of non coding processing intermediates (By similarity). Confers salinity and drought stress tolerances by maintaining both photosynthesis and antioxidant machinery, probably via an increase in plant hormones levels such as gibberellic acid (GA(3)), the cytokinin zeatin (Z) and indole-3-acetic acid (IAA) (, ).
Subcellular locations: Nucleus, Mitochondrion matrix, Mitochondrion matrix, Mitochondrion nucleoid |
SYAP_ORYSI | Oryza sativa subsp. indica | MEAAALLSPTATSRSPLPLLSTAPAAHRLHVLLPLSGRRRRLCLRSSPRPRGSLGCAGDCVVRSMGSSRERGVLVKTSSSSASVESATQEVGAASSGEWSGDAIRRRFLDFYAARGHKILPSSSLVPDDPTVFLTIAGMLQFKPIFLGKEPRRVPCATTSQKCIRTNDIENVGRTSRHQTFFEMLGNFSFGDYFKKEAITWAWELTTKEFGLPPERLWISVFQDDDEAFSIWHNEVGVPKERIKRLGEDDNFWTSGATGPCGPCSEIYYDFYPERGSSDADLGDDSRFIEFYNLVFMQYNKKDDGSLEPLKQKNIDTGMGLERMARILQKVPNNYETDLIFPIIEKAASMALVSYTTADDAMKTNLKIIGDHMRAVVYLISDGVIPSNIGRGYVVRRLIRRVVRTGRLIGIRGDGHGNSEGAFLPSLAEVAISLSTEIDPDVESRRKSILGELQREELRFVQTLERGEKLLDELLDEALSSAGNNGGKPCLSGKDVFLLYDTYGFPVEITAEIAGERGVIVDMKGFDMEMENQRKQSQAAHNVVKLSVGNETEIVKSIPDTEFLGYDSLSATAVVKGLLVNGNSVNVVSEGSDVEIFLDRTPFYAESGGQVGDNGFLYVYGEEDAKQKAVIEINDVQKSLGNIFVHKGTIKQGSVEVGKEIDAAVDAKLRQGAKAHHTATHLLQSALKSIIGSETSQAGSLVAFDRLRFDFNFHRPLSEEELMKIESLVNQWVSSATHLETKVMDLQDAKNAGAIAMFGEKYGEQVRVVEVPGVSMELCGGTHVSNTAEIRGFKIISEQGIASGVRRIEAVAGDAFVEYVCARDNYMRCLCSSLKVKAEDVNGRVETILEELRTTRNEVSSLRSKIAVLKAASLANKATTIDNTRVVVENMGDVDADGLKSAAEYLVDTLEDPAAVILGSSPGDGKVSLVAAFSPGVVKMGIQAGKFVGGIAKLCGGGGGGKPNFAQAGGRKPENLPGALEKARDEIVAAISSKSS | Catalyzes the attachment of alanine to tRNA(Ala) in a two-step reaction: alanine is first activated by ATP to form Ala-AMP and then transferred to the acceptor end of tRNA(Ala). Also edits incorrectly charged tRNA(Ala) via its editing domain.
Subcellular locations: Plastid, Chloroplast, Mitochondrion |
SYAP_ORYSJ | Oryza sativa subsp. japonica | MEAAALLSPTATSRSPLPLLSTAPAAHRLHVLLPLSGRRRRLCLRSSPRPRGSLGCAGDCVVRSMGSSRERGVLVKTSSSSASVESATQEVGAASSGEWSGDAIRRRFLDFYAARGHKILPSSSLVPDDPTVFLTIAGMLQFKPIFLGKEPRRVPCATTSQKCIRTNDIENVGRTSRHQTFFEMLGNFSFGDYFKKEAITWAWELTTKEFGLPPERLWISVFQDDDEAFSIWHNEVGVPKERIKRLGEDDNFWTSGATGPCGPCSEIYYDFYPERGSSDADLGDDSRFIEFYNLVFMQYNKKDDGSLEPLKQKNIDTGMGLERMARILQKVPNNYETDLIFPIIEKAASMALVSYTTADDAMKTNLKIIGDHMRAVVYLISDGVIPSNIGRGYVVRRLIRRVVRTGRLIGIRGDGHGNSEGAFLPSLAEVAISLSTEIDPDVESRRKSILGELQREELRFVQTLERGEKLLDELLDEALSSAGNNGGKPCLSGKDVFLLYDTYGFPVEITAEISGERGVIVDMKGFDMEMENQRKQSQAAHNVVKLSVGNETEIVKSIPDTEFLGYDSLSATAVVKGLLVNGNSVNVVSEGSDVEIFLDRTPFYAESGGQVGDNGFLYVYGEEDAKQKAVIEINDVQKSLGNIFVHKGTIKQGSVEVGKEIDAAVDAKLRQGAKAHHTATHLLQSALKSIIGSETSQAGSLVAFDRLRFDFNFHRPLSEEELMKIESLVNQWVSSATHLETKVMDLQDAKNAGAIAMFGEKYGEQVRVVEVPGVSMELCGGTHVSNTAEIRGFKIISEQGIASGVRRIEAVAGDAFVEYVCARDNYMRCLCSSLKVKAEDVNGRVETILEELRTTRNEVSSLRSKIAVLKAASLANKATTIDNTRVVVENMGDVDADGLKSAAEYLVDTLEDPAAVILGSSPGDGKVSLVAAFSPGVVKMGIQAGKFVGGIAKLCGGGGGGKPNFAQAGGRKPENLPGALEKARDEIVAAISSKSS | Catalyzes the attachment of alanine to tRNA(Ala) in a two-step reaction: alanine is first activated by ATP to form Ala-AMP and then transferred to the acceptor end of tRNA(Ala). Also edits incorrectly charged tRNA(Ala) via its editing domain.
Subcellular locations: Plastid, Chloroplast, Mitochondrion |
SYAP_SORBI | Sorghum bicolor | MEVAAVSATSRPLSPLLSTAPARRLRLLPPRCVFGRRLRASPRTRASVEPATQELGTAGAGEWSGDAIRRRFLEFYAARGHKILPSSSLVPDDPTVLLTIAGMLQFKPIFLGKEPRRVPCATTSQKCIRTNDIENVGRTARHQTFFEMLGNFSFGDYFKKEATAWAWELATKEYGLPAERLWISVFEDDNEAFDIWHNEVGVPKERIKRMGAEDNFWTSGATGPCGPCSEIYYDFYPERGSSDADLGDDSRFIEFYNLVFMQYNKKDDGSLEPLKQKNIDTGMGLERMARILQKVPNNYETDLIFPIIEKAASMAMVSYAKTDDATKTNLKIIGDHMRAVVYLVSDGVIPSNIGRGYVVRRLIRRVVRMGRLIGIRGDGHGNSEGAFLPSLAEVVISLSTEIDPDVESRRRSILGELQREELRFVQTLERGEKLLDELLDGAVLSAGNNGDKPSLSGKDLFLLYDTYGFPVEITAEIASERGVTVDIEGFDIEMENQRKQSQAAHNVVKLSVGNETEIIKSIPDTVFLGYDSLSASAVVRGLLVNGNPVNEVSEGSEVEILLDRTPFYAESGGQVGDNGFLYVNGGEDRSQAAVIEINDVQKSLGNIFVHKGTIKQGSVEVGKEVDACVDAKLRQGAKAHHTATHLLQSALKSVVGSETSQAGSLVAFDRLRFDFNFHRPVSEGELTRIELLVNQWISNAAHLETKVMALQDAKNAGAIAMFGEKYGEQVRVVEVPGVSLELCGGTHVSNTAEIRGFKIISEQGIASGIRRIEAVAGDAFIDYVCARDNYMRRLCSSLKVKAEDVNGRVETILEELRATRNEVSSLRSKIAVLKAASLASKATTVEPQNVRIVVENMGDVDADGLKSAAEYLIGTLQDPAAVILGSSPGDGKVSLVAAFSPAVVKMGLQAGKFVGGIAKLCGGGGGGKPNFAQAGGRKPENLPDALEKARAEIVAGVSSSS | Catalyzes the attachment of alanine to tRNA(Ala) in a two-step reaction: alanine is first activated by ATP to form Ala-AMP and then transferred to the acceptor end of tRNA(Ala). Also edits incorrectly charged tRNA(Ala) via its editing domain.
Subcellular locations: Plastid, Chloroplast, Mitochondrion |
SYK_SOLLC | Solanum lycopersicum | MDSSVSTEPLSKNALKREKKAKEKEQLEQEKKAAAVAKRQMEQHNLPENDDLDPTQYLANRLRNIESLRESGINPYPHKFFITMSIPEFISRYAHLNTGEFPEDIDMSLAGRVISKRASSSKLYFYELLGGGARVQVLASARDSDVDAVQFSNYQSGVKRGDIIGVRGYPGKSKRGELSIFAKPFIVLAPCLHMLPRRLTSSIVDETRTQNFQGITAYDTWTPGDLRNPESYVLRDQETRYRQRYLDLMMNPEVRALFRTRARIISYIRSFLDNLEFLEVETPSMNLTAGGASARPFITHHNELDTELLIRVSPELYLKKLVVGGFDRVYELGKHFRNEGMDLTHSPEFTMCELYMAYADYNDLMDLTEQLLSGMVKDLTGSYKIRYHANGLDNEPIEIDFTPPFRKIDMLSELEKVANISIPRDLSSESANKHLVDVCEKFDVKCPPPHTTTRLLDKLVGHFIEVNCINPTFIINHPEIMSPLAKSRRSEPGLTERFNLFVNRRELCDAYTELNDPTAQRERFAEQLKDRQLGDDEAMDLDESFITALEYGLPPTGGLGMGIDRLTMLLTDSQNVKEVILFPAMRLQ | Subcellular locations: Cytoplasm |
TADA2_ORYSJ | Oryza sativa subsp. japonica | MGRSRGVPNSGDDETNHRSKRRRVASSGDAPDSLSAACGGAGEGGGKKALYHCNYCNKDISGKIRIKCSKCPDFDLCVECFSVGAEVTPHRSNHPYRVMDNLSFPLICPDWNADEEILLLEGIEMYGLGNWAEVAEHVGTKTKAQCIDHYTTAYMNSPCYPLPDMSHVNGKNRKELLAMAKVQGESKKVLPGDLTPKDESPFSPPRVKVEDALGEGLAGRSPSHIAGGANKKASNVGQFKDGANVAKVEDGHVDRSIGVKKPRYSADEGPSLTELSGYNSKRHEFDPEYDNDAEQALAEMEFKETDSETDRELKLRVLRIYLSRLDERKRRKEFILERNLLFPNPLEKDLTNEDKEVYHRYKVFMRFLSKEEHEALVRSVLEERKIRRRIQELQECRSAGCRTLAEAKIHIEQKRKKEHEVNAQKAKESGQLLSNTKVVHKTNRPMKIESDGNLDQKKGGASLDSTGRDSPKTTGHAGTKHWDDWDIVGFPGAELLSTSEKNLCCQNRLLPNHYLKMQEVLMQEIFKGSVAKKEDAHVLFKVDPAKVDNVYDMVTKKLGTNEEAPTV | Required for the function of some acidic activation domains, which activate transcription from a distant site (By similarity). The exact mechanism of action is not yet known (By similarity). ADA2 and GCN5 function to acetylate nucleosomes, opening up the promoter region . The ADA2-GCN5 histone acetyltransferase (HAT) module is recruited by WOX11 to regulate crown root cell proliferation and stem cell maintenance of root meristem . The ADA2-GCN5 HAT module together with WOX11 targets and regulates a set of root-specific genes involved in carbon metabolism, cell wall biosynthesis, and auxin transport and response .
Subcellular locations: Nucleus
Expressed in roots, mature leaves, stems and panicles. |
TAF1B_ORYSI | Oryza sativa subsp. indica | MDDDGGGSPGHYGGGGIHLVCEYCGHGSEYAEDDADNGFFTCRQCSAIHTSTQNTATNPFDFPMTPAHLSAHRRPTQPTPTPKPFPAPRGAATGAAAPDFDDLGEPSEPRDFATGANAWGNPEDVAARVRWRYVRGLQVILQRQLEALVERHRVGSLAASLAGTIWLRWVAASKVFDEMWVHKMLAIAASVEEGHSASKDKQSELEGDAQKSQSSYEFLFLRSLRMMLPVYSTLAVCFLACHVARETILPTDICRWAMEGKLPYVAAFTQVDKLLGSSLNDCPLSSRQLFRPTRVIGAWQLEAAAGSIAQKIGLLLPSVNFYLIAQRFLKELSLPIEKILPHACRIYEWAMPAELWLSSNPGRVPSRVCVMAILIVALRVLYGINGQGIWESIAQTENAVGSDPEASAPHSIEPDSNNSEEFDARELLCTLAASYDKIDVGHDYSKEVHSYLKYCKDVVFTGMTFSLEEEHLIDIFWDMYKGKEVMLLDENAKLCQEKLRTTNGVNKRCRDGRFADTKCCSTPLGNCALQSIKSKMEENGFCYVSPRKRLVSDGYLLYTRRESSGSLIYVAHADYYILLRPFAKLAEVDVRVLHSSVLKLERRLGWIEERVGRSLNTLQNLHDEASDDERPVSD | Component of RNA polymerase I core factor complex that acts as a GTF2B/TFIIB-like factor and plays a key role in multiple steps during transcription initiation such as pre-initiation complex (PIC) assembly and postpolymerase recruitment events in polymerase I (Pol I) transcription. Binds rDNA promoters and plays a role in Pol I recruitment (By similarity).
Subcellular locations: Nucleus, Nucleolus |
TAF1B_ORYSJ | Oryza sativa subsp. japonica | MDDDGGGSPGHYGGGGIHLVCEYCGHGSEYAEDDADDGFFTCRQCSAIHTSTQNTATNPFDFPMTPAHLSAHRRPTQPTPTPKPFPAPRGAATGAAAPDFDDLGEPSEPRDFATGANAWGNPEDVAARVRWRYVRGLQVILQRQLEALVERHRVGSLAASLAGTIWLRWVAASKVFDEMWVHKMLAIAASVEEGHSASKDKQSELEGDAQKSQSSYEFLFLRSLRMMLPVYSTLAVCFLACHVARETILPTDICRWAMEGKLPYVAAFTQVDKLLGSSLNDCPLSSRQLFRPTRVIGAWQLEAAAGSIAQKIGLLLPSVNFYLIAQRFLKELSLPIEKILPHACRIYEWAMPAELWLSSNPGRVPSRVCVMAILIVALRVLYGINGQGIWESIAQTENAVGSDPEASAPHSIEPDSNNSEEFDARELLCTLAASYDKINVGHDYSKEVHSYLKYCKDVVFTGMTFSLEEEHLIDIFWDMYKGKEVMLLDENAKLCQEKLRTTNGVNKRCRDGRFADTKCCSTPLGNCALQSIKSKMEENGFCYVSPRKRLVSDGYLLYTRRESSGSLIYVAHADYYILLRPFAKLAEVDVRVLHSSVLKLERRLGWIEERVGRSLNTLQNLHDEASDDERPVSD | Component of RNA polymerase I core factor complex that acts as a GTF2B/TFIIB-like factor and plays a key role in multiple steps during transcription initiation such as pre-initiation complex (PIC) assembly and postpolymerase recruitment events in polymerase I (Pol I) transcription. Binds rDNA promoters and plays a role in Pol I recruitment (By similarity).
Subcellular locations: Nucleus, Nucleolus |
TALDO_CAPAA | Capsicum annuum var. annuum | GVTSNPAIFQKAISTSNAYNDQFR | Transaldolase is important for the balance of metabolites in the pentose-phosphate pathway.
Subcellular locations: Cytoplasm |
TBB4_MAIZE | Zea mays | MREILHIQGGQCGNQIGAKFWEVICGEHCVDSTGRYSGTSSQQLELERINVYYNEAGGGRYVPRAVLMDLEPGTMESIRAGPFGGIFRPDNFVYGQSGAGNNWAKGHYTEGAELIDSVLDVVRKEAENCDCLQGFQVCHSLGGGTGSGMGTLLISKIREEYPDRMMLTFSVFPSPKVSDTVVEPYNATLSVHQLVENADECMVLDNEALYDICFRTLKLTNPSFGDLNHLISATMSGVTCCLRFPGQLNSDLRKLAVNLIPFPRLHFFMVGFAPLTSRGSQQYRALTVPELTQQMWDAKNMMCSADPRHGRYLTASAMFRGKMSTKEVDEQMINVQNKNSSYFVEWIPNNVKSSVCDIPPVGLPMASTFVGNSTSIQEMFRRVSEQFTAMFRRKAFLHWYTSEGMDEMEFTEAESNMNDLVAEYQQYQDATAEEYEEEEHDGEEEHA | Tubulin is the major constituent of microtubules, a cylinder consisting of laterally associated linear protofilaments composed of alpha- and beta-tubulin heterodimers. Microtubules grow by the addition of GTP-tubulin dimers to the microtubule end, where a stabilizing cap forms. Below the cap, tubulin dimers are in GDP-bound state, owing to GTPase activity of alpha-tubulin.
Subcellular locations: Cytoplasm, Cytoskeleton |
TBB4_ORYSJ | Oryza sativa subsp. japonica | MREILHIQGGQCGNQIGAKFWEVVCDEHGIDPTGRYTGNSDLQLERVNVYYNEASCGRFVPRAVLMDLEPGTMDSVRTGPYGQIFRPDNFVFGQSGAGNNWAKGHYTEGAELIDSVLDVVRKEAENCDCLQGFQVCHSLGGGTGSGMGTLLISKIREEYPDRMMLTFSVFPSPKVSDTVVEPYNATLSVHQLVENADECMVLDNEALYDICFRTLKLTTPSFGDLNHLISATMSGVTCCLRFPGQLNSDLRKLAVNLIPFPRLHFFMVGFAPLTSRGSQQYRALTVPELTQQMWDAKNMMCAADPRHGRYLTASAMFRGKMSTKEVDEQMINVQNKNSSYFVEWIPNNVKSSVCDIPPRGLSMASTFIGNSTSIQEMFRRVSEQFTAMFRRKAFLHWYTGEGMDEMEFTEAESNMNDLVSEYQQYQDATADEEGEYEDEEQQEADDM | Tubulin is the major constituent of microtubules, a cylinder consisting of laterally associated linear protofilaments composed of alpha- and beta-tubulin heterodimers. Microtubules grow by the addition of GTP-tubulin dimers to the microtubule end, where a stabilizing cap forms. Below the cap, tubulin dimers are in GDP-bound state, owing to GTPase activity of alpha-tubulin.
Subcellular locations: Cytoplasm, Cytoskeleton
Expressed in roots and leaf sheaths. |
TBB4_WHEAT | Triticum aestivum | MREILHIQGGQCGNQIGAKFWEVICDEHGIDGTGRYAGDSDLQLERINVYYNEASGGRFVPRAVLMDLEPGTMDSVRSGPFGQIFRPDNFVFGQSGAGNNWAKGHYTEGAELIDSVLDVVRKEAENCDCLQGFQVCHSLGGGTGSGMGTLLISKIREEYPDRMMLTFSVFPSPKVSDTVVEPYNATLSVHQLVENADECMVLDNEALYDICFRTLKLATPSFGELNHLISATMSGVTCCLRFPGQLNSDLRKLAVNLIPFPRLHFFMVGFAPLTSRGSQMYRALTVPELTQQMWDAKNMMCAADPRHGRYLTASACFRGKMSTKEVDEQMLNVQNKNSSYFVEWIPNNVKSSVCDMPPRGLKMAGTFVGNSTSIQEMFRRVSEQFTAMFRRKAFLHWYTGEGMDEMEFTEAESNMNDLVAEYQQYQDATADEEYDEEEEEERDAE | Tubulin is the major constituent of microtubules, a cylinder consisting of laterally associated linear protofilaments composed of alpha- and beta-tubulin heterodimers. Microtubules grow by the addition of GTP-tubulin dimers to the microtubule end, where a stabilizing cap forms. Below the cap, tubulin dimers are in GDP-bound state, owing to GTPase activity of alpha-tubulin.
Subcellular locations: Cytoplasm, Cytoskeleton |
TBT1_ORYSJ | Oryza sativa subsp. japonica | MEITSSAMLKTTTTPPHPLAGEKVPLSAFDRAAFDVFVPLVFAYRAPAPSSEAVKEGLRVAVAAYPLVSGRIAVDGQGRRRRRRVLHVNNEGVLVLDATVEVDLDAVLAANVATDLYPALPEHSFGAALLQVQLTRFGCGGLVVGLIGHHHVFDGHSMSTFCATWARAVRDSEAFIVPSPSLDRAITGVPRSPPAPVFDHRSIEFKVGNKSSDSSGAAAAAAVEKIANIGVRFTAKFVAELKARVGGRCSTFECVLAHAWKKITAARGLKPEEFTRVRVAVNCRRRANPPAPADLFGNMVLWAFPRLQVRRLLSSSYRDVVGAIRAAVARVDAEYIQSFVDYVEVADARGEELAATAAEPGETLCPDLEVDSWLGFRFHEMDLGTGPPAAVLSPDLPIEGLMILVPVGGDGGGVDLFVALADDHAQAFEQICYSLEEHAMIHSHL | Hydroxycinnamoyl transferase that catalyzes the transfer of an acyl from benzoyl-CoA to tryptamine, to produce benzoyl tryptamine. Serotonin and tyramine serve as acyl acceptors in vitro. Can use p-coumaroyl-CoA, and to a lesser extent caffeoyl-CoA, as acyl donors. |
TBT2_ORYSJ | Oryza sativa subsp. japonica | MEITSSAMLKPAPTPTPHPLAGEKVPLTAFDRAAFDVFVPMVFAYRAPAPSSEAVKEGLRMAVAAYPLAAGRLAVDVAADGQGRRRRRRVLHVNDEGALVLDATVEADLDAVLAANVATDLYPAPPEHSFGAAVLQVQLTRFRCSGLVVGLIVHHHVFDGHSTSAFCTTWARAVRDGEAFSVPSPCLDRAITSVPRSPPAPVFDHRSIEFKVGNKSSDSSGAAAAAVEKITNIGVRFTAKFVAELKARVGGRCSTFECVLAHAWKKMTAARGLKPEEFTRVRVAVNCRRRANPPAPADLFGNMVLWAFPRLQVRRLLSASYRDVVGAIRAAVARVDGEYIQSFVDYVEVADARGEELAATAAEPGETLCPDLEVDSWLGFRFHEMDLGTGPPAAVLSPDLPIEGLMILVPVGGDGGGVDLFVALADDRAQVFEQICYSLEEHAIPSHL | Hydroxycinnamoyl transferase that catalyzes the transfer of an acyl from benzoyl-CoA to tryptamine, to produce benzoyl tryptamine. Serotonin and tyramine serve as acyl acceptors in vitro. Specific for benzoyl-CoA as acyl donor. Has no activity with p-coumaroyl-CoA, caffeoyl-CoA, or feruloyl-CoA as acyl donors. |
TERT_ORYSJ | Oryza sativa subsp. japonica | MPRRRRRRRAAPGGQVPPELRLAYGARALTLGRAVFSLLPSPRHCESPCPACRGRVASGCLACRRWEHLLRDGDPVAYRRLITRAVCAIAADDLSAPPPPRYTPGNSGHSQARLVREMMKSIVADQSHGTKNVLCNGLHEGGQSICISDLVSSSSWSILLHRIGDLLMCYLLRCTSIFLPVKKNDYFQVSGVPLNVVLRNPIFASTVARKHQPQTTKAKCHTCYLWKSANMAENLSICHDSSNSGVNSSFSSTCKIVTQQSCETCGSIRRAESKDPSEGCNCPKFPSDGRSGECCNCYTHNTRKRKRLYSWQRRSKKKQVCSVDESSAEWSKLNGSNFNMSNGPSENLAGKMNDQAQSVELTVDNTSLARSNDDSSSEIKVINATILSSEKSPCSVFDIRGSQGLSCHYSLSEVQYQSTCPQVGPSSYLHLNSCSICFNCIISNASKHLSLDSLISRNGIFYNRRTTYSVFHCKHILSKRKRPDALSLVKHIFGINSCCASLLKYNCHESTIRKSNCLCCWLPKSIKNLIRNSKRCQYKKLFLKHCSVKCKVAPDVTKNDGKAHYPPGGKAAYYDRSFSRLEAYSTHQQVASFVWAVLKRIVPKPLLGNSFGKRSLRTNIWKFIKLRRFETFQLSDCIGDLKVSHYSWLSNIEFSNCFCSAIIGKQTGSSTSAEEQKQKNILHCWISWLFSDIVIPVVRTYFYVTERESKRYDVFYYPKSVWRDLTSNAIASLNKKNFRILRGEPRKAVRHLNCSSRVRFLPKAKDMRPLVDLRAKSKDANLNKCHLIMKKLRDEKPEMFGSSVFDYNNVHQNLSQFISSKRSQLMKKLKVYIVVADVSKAFDCVSHDMVLKMIDDAFKCDEYTVRKCSKVICNRSKNSLYRFDSNASIGNGNSIYDLSIQLSSGGGIFVDQGTICRILKEQFHHLLYEQIKCNILKIGQKYYLQQVGIAQGSKLSPNLCSLYYGHLENSVLSKFLHDSKLNAGEAFSEPEYLLMRFIDDFIFISFSLEHAQKFLNRMRRGFVFYNCYMNDSKYGFNFCAGNSEPSSNRLYRGDDGVSFMPWSGLLINCETLEIQADYTRYLDITIISTITVKMHSSTKYIHSKLCHYMRPKCHPIFYDSNINSPGTIRVNIYQAFLLCAMKFHCYIRSVSDANVSKLELLQVIKRTFRYMHSLIVRRMQDVELHYNVRPVLKLRRKETIWLGLTAYIRVLQQKQSRYKDMLTLLTAELGRYCHLGHECDTLRYAVDDSHSSMFWKFKF | Telomerase is a ribonucleoprotein enzyme essential for the replication of chromosome termini in most eukaryotes. It elongates telomeres. It is a reverse transcriptase that adds simple sequence repeats to chromosome ends by copying a template sequence within the RNA component of the enzyme (By similarity).
Subcellular locations: Nucleus, Chromosome, Telomere
Expressed in shoot apices and immature embryos. |
THF1_ORYSJ | Oryza sativa subsp. japonica | MAAISSLPFAALRRAADCRPSTAAAAAGAGAGAVVLSVRPRRGSRSVVRCVATAGDVPPTVAETKMNFLKSYKRPILSIYSTVLQELLVQQHLMRYKTTYQYDAVFALGFVTVYDQLMEGYPSNEDRDAIFKAYITALNEDPEQYRADAQKMEEWARSQNGNSLVEFSSKDGEIEAILKDISERAQGKGSFSYSRFFAVGLFRLLELANATEPTILDKLCAALNINKRSVDRDLDVYRNILSKLVQAKELLKEYVEREKKKREERSETPKSNEAVTKFDGSLNSMRH | Involved in a dynamic process of vesicle-mediated thylakoid membrane biogenesis. Required for the normal organization of vesicles into mature thylakoid stacks and ultimately for leaf development (By similarity).
Subcellular locations: Plastid, Chloroplast outer membrane, Plastid, Chloroplast stroma |
THN2_WHEAT | Triticum aestivum | MGSKGLKGVMVCLLILGLVLEQVQVEGKSCCRTTLGRNCYNLCRSRGAQKLCSTVCRCKLTSGLSCPKGFPKLALESNSDEPDTIEYCNLGCRSSVCDYMVNAAADDEEMKLYVENCGDACVNFCNGDAGLTSLDA | Thionins are small plant proteins which are toxic to animal cells. They seem to exert their toxic effect at the level of the cell membrane. Their precise function is not known.
Subcellular locations: Secreted |
THN3_HORVU | Hordeum vulgare | MAPSKSIKSVVICVLILGLVLEQVQVEGKSCCKDTLARNCYNTCHFAGGSRPVCAGACRCKIISGPKCPSDYPKLNLLPESGEPDVTQYCTIGCRNSVCDNMDNVFRGQEMKFDMGLCSNACARFCNDGAVIQSVEA | Thionins are small plant proteins which are toxic to animal cells. They seem to exert their toxic effect at the level of the cell membrane. Their precise function is not known.
Subcellular locations: Secreted |
THN5_HORVU | Hordeum vulgare | MATNKSIKSVVICVLILGLVLEQVQVEAKSCCKNTTGRNCYNACRFAGGSRPVCATACGCKIISGPTCPRDYPKLNLLPESGEPNATEYCTIGCRTSVCDNMDNVSRGQEMKFDMGLCSNACARFCNDGEVIQSVEA | Thionins are small plant proteins which are toxic to animal cells. They seem to exert their toxic effect at the level of the cell membrane. Their precise function is not known.
Subcellular locations: Secreted |
THN5_WHEAT | Triticum aestivum | MGGGQKGLESAIVCLLVLGLVLEQVQVEGVDCGANPFKVACFNSCLLGPSTVFQCADFCACRLPAGLASVRSSDEPNAIEYCSLGCRSSVCDNMINTADNSTEEMKLYVKRCGVACDSFCKGDTLLASLDD | Thionins are small plant proteins which are toxic to animal cells. They seem to exert their toxic effect at the level of the cell membrane. Their precise function is not known.
Subcellular locations: Secreted
Developing endosperm. |
THN6_HORVU | Hordeum vulgare | MAPSKSIKSVVICVLILVLVLEQVQVEGKSCCKDTLARNCYNTCRFAGGSRPVCAGACRCKIISGPKCPSDYPKLNLLPESGEPDVTQYCTIGCTNSVCDNMDNVFRGQEMKFDMGLCSNACARFCNDGAVIQSVEA | Thionins are small plant proteins which are toxic to animal cells. They seem to exert their toxic effect at the level of the cell membrane. Their precise function is not known.
Subcellular locations: Secreted |
THN7_HORVU | Hordeum vulgare | MATNKSIKSVVICVLILGLVLEQVQVEGKSCCKNTTGRNCYNACRFAGGSRPVCATACGCKIISGPTCPRDYPKLNLLPESGEPNVTEYCTIGCRTSVCDNMDNVSRGQEMKFDMGLCSNACARFCNDGEVIQSVEA | Thionins are small plant proteins which are toxic to animal cells. They seem to exert their toxic effect at the level of the cell membrane. Their precise function is not known.
Subcellular locations: Secreted |
THNA_HORVU | Hordeum vulgare | MVCLLILGLVLEQVQVEGKSCCRSTLGRNCYNLCRVRGAQKLCAGVCRCKLTSSGKCPTGFPKLALVSNSDEPDTVKYCNLGCRASMCDYMVNAAADDEEMKLYLENCGDACVNFCNGDAGLTSLTA | Thionins are small plant proteins which are toxic to animal cells. They seem to exert their toxic effect at the level of the cell membrane. Their precise function is not known.
Subcellular locations: Secreted |
THNB_HORVU | Hordeum vulgare | MGSKGLKGVMVCLLILGLVLEHVQVEGKSCCRSTLGRNCYNLCRVRGAQKLCANACRCKLTSGLKCPSSFPKLALVSNSDEPDTIDYCNLGCRASMCDYMVNAAADDEEMKLYVEHCSDACVNFCNGDVGLTSLTA | Thionins are small plant proteins which are toxic to animal cells. They seem to exert their toxic effect at the level of the cell membrane. Their precise function is not known.
Subcellular locations: Secreted |
THNB_WHEAT | Triticum aestivum | MGSKGLKGVMVCLLILGLVLEQVQVEGKSCCKSTLGRNCYNLCRARGAQKLCANVCRCKLTSGLSCPKDFPKLVLESNSDEPDTMEYCNLGCRSSLCDYIVNAAADDEEMKLYVEQCGDACVNFCNADAGLTSLDA | Thionins are small plant proteins which are toxic to animal cells. They seem to exert their toxic effect at the level of the cell membrane. Their precise function is not known.
Subcellular locations: Secreted |
TI214_PHAVU | Phaseolus vulgaris | MIFESFILENLVFLCMKIMNSIVVVGLYYGFMTTFSIGPSYLFLLRARLVEEGTENKISATTGFITGQLIIFMSIYYAPLHLALGRPHTITVIAIPYLLFQFFGNSKKNFLNYGYKNPNSIRNFSIQRIFFQNLLFQFFNPLFLPSSIFMRFVNIYLFRCNNKVLFLTSSFIGWIIGHTFFMKWIEFLLICIQQNNLIKSNVRIQSNKYILSELKNSMFQIFVVFLFVTCLYYLGRIPPPFFSKKLLEIKESNEFFKKEKKGDVETNLQRIRTKQKRSNNKDIFPSIFLKKEKNLYKLDEQKNKLQKPLLNILFNYKRWNRPFRYIKNNQFENIIKNEISEFFFHTYPRNGREKIYFTYPQNLSTFQKMMETKIDIFTIKKISYDDSSNHSSYSNEEKRKKLSNEFITRTKLIDKELISLDIFENRIRLCNDETKKNYFTKITDPFLNGPFRGRIKKGFSTSIQDEKTYKKNHILINKIQEIFLYNSKKIPKKNNRNYQKLEENLKTFNKKLLVTTFLFNLISQFSKKSVSSFNYEVLYLFPEHEQVKMNSNLEEEKKLIIKILFDAITTDLNEKTKGNRNNTKSIKINEICKKVPRWSYKFMDELEELGGKMEADNSQIRSRKAKRVVILTNKSKFFKKYNTYNDLGDTENTENTEKKNELALRRYSQQSDFRRDIIKGSIRAQRRKTVTWKFFQKRVHSPLFLDKIEKSLFFSFDTFKSMKIFLKLKIWIRKKTEFKILGYIEEKTKKSPKKEEEKKKGNEERKRIEIAEAWDSIIFAQVIRGVLLITQCIIRKYILLPSLIIIKNMIRILFFQIPEWSEDYRDWKRERYIKCTYNGVQLSEREFPQKWLTDGIQIKIVFPFHLKPWHKYKIRCNKKKKDSKKKKNFCFLTVWGMEVELPFSSSPKNLFSFFDPILKELKKKTKQFEFFTFRVLKVFSEKFKLFLNIVIEKAKWIINRIMESLKKSIVFLTKKRKEFFESLFIQWKPKKLDELSENKIDEATISIQSIKSTNFALKKKKIKDLNTKRKVVIKKIKKLKKEEKKRGLVISETNIDSNKTISDSKRIEFEKKNLQILKRIHIRLTKKSHSFLKFFIKKIYLDIFLYIICIPKIHIQPFIESTKKFLNKWIYGNETNAERTYKTNQSIIPFISKLHKYFHNRNLNSHNYFDVSFLSQAYVFFNLLQTRIININIYKLRLLFEYHKNFFFVKNKIKNSFFGAQGIVHSKLEQKNLLNSKRNQWTNWLKNHYYQYDLSNSRWSKLLSQKWRNRITKFGVAQNPNLTKWDSYGKSPLIIYKEQQGAALKKKIRKQYRYDLLSYNFMNYANKKDSYIYGYRSLFQSNKNIWISSNYNTYKKNLFDRISNIFIKNYEDAIIIDIEKNSNRKYLDWMGIHREILNRSISNPEFWFFSKFVIFYNAYRSNSQIIPIKLLYLHSKVSKVNKNVSEKNITRKKKRIAVFRASKKQEDIEKNSVAVGRGSEKNSYVIKKKKVKNNMEVELHFLVRNFLIFHFNWKNFLGQNIFHNVKVYCLLIRLTNLRKMTIASIQRGELGLDIMIIQNQKNLTLPGLSKNKNNKLRKKELFVIEPVRLSRKNNKQFLKSKTMDLSLIHKNKRKIDKKYLKKIHVNKKSFYKYITRTRDQKITEKNEKEILNFLVPENILSARRRRELRMRICLYPNNRNSIHRNTIFDNENKVKKGFQVLTKKRNEKEKKKLMNFKIFLWPKYRLEDLACINRYWFNTHNGSRFSIVRIHLYPRVKIC | Involved in protein precursor import into chloroplasts. May be part of an intermediate translocation complex acting as a protein-conducting channel at the inner envelope.
Subcellular locations: Plastid, Chloroplast inner membrane |
TIM9_ORYSJ | Oryza sativa subsp. japonica | MDKSMLGDLDGLPEEDKMRMAAMVDQLQIRDSLRMYNSLVERCFTDCVDTFRRKTLDKQEESCVRRCAEKFLKHSMRVGMRFAELNQGVATPD | Mitochondrial intermembrane chaperone that participates in the import and insertion of multi-pass transmembrane proteins into the mitochondrial inner membrane. May also be required for the transfer of beta-barrel precursors from the TOM complex to the sorting and assembly machinery (SAM complex) of the outer membrane. Acts as a chaperone-like protein that protects the hydrophobic precursors from aggregation and guide them through the mitochondrial intermembrane space (By similarity).
Subcellular locations: Mitochondrion inner membrane |
TL20_SPIOL | Spinacia oleracea | RDVDVGSFLPKSPSDPSMVL | Subcellular locations: Plastid, Chloroplast thylakoid lumen |
TL22_SPIOL | Spinacia oleracea | EQSAGFREYIDFFDGYSLTY | Subcellular locations: Plastid, Chloroplast thylakoid lumen |
TL25_SPIOL | Spinacia oleracea | AIANAPLLDTTITDRVFFD | Subcellular locations: Plastid, Chloroplast thylakoid lumen |
TL29_SOLLC | Solanum lycopersicum | MVSFASTLPSLVSFIPSPSSITNASRNPPQPGMICCKFRSELNNEDRFHRRDILQSVGAAVGMDLIARSSAFIEVANAADLIQRRQRSDFQSKIKLTLYDAIKANPDIIPSLLTLALNDAITYDKATKTGGPNGSIRFSSEISRPENKGLDAALNLLEESKKVIDLDSKGGPISYADLIQFAAQSAVKSTFIASAISKCGGNVEKGTLLYSAYGSNGQWGQFDRIFGRSDAQEPDPEGRVPQWDKASVQEMKDKFKAVGLGPRQLAVMSSFLGPDQAATEALLASDPEVLPWIQKYQRSRETVSRTDYEVDLITTVTKLSSLGQVINYEAYTYPPRKIDVTKLKL | Subcellular locations: Plastid, Chloroplast thylakoid lumen |
TL29_SPIOL | Spinacia oleracea | ADLIQRRQRSEFQSDIKGILYTVIKKNPDL | Subcellular locations: Plastid, Chloroplast thylakoid lumen |
TL33_SPIOL | Spinacia oleracea | VLYSPDTKVPR | Subcellular locations: Plastid, Chloroplast thylakoid lumen |
TLC1_SOLTU | Solanum tuberosum | MEGVLQTRGLLSLPSKPKIKAFYPLPQGGLRNRFNSLSSLKPNPLNGVSLSSNGFQKVQGFDTKPQLFGQKKRCFPICKAEAAAAAGAADGQPLFVEKEQPKFMGIELVTLKKIIPLGAMFFCILFNYTILRDTKDVLVVTAKGSSAEIIPFLKTWVNLPMAIGFMLLYTKLANVLSKEALFYTVILPFIAFFGAFGFVLYPLSNYFHPTAFADKLLNTLGPRFLGPIAILRIWSFCLFYVMAELWGSVVVSVLFWGFANQITTVDEAKRFYPLFGLGANVALIFSGRTVKYFSSLRSSLGPGVDGWAISLKGMMSIVVMMGGAICFFYWWVNRNVALPTRSKKKKVKPNMTTMESLKFLVSSKYIRDLATLVVAYGISINLVEVTWKSKLKAQFPSPNEYSSFMGDFSTATGIATFTMMLLSQWIFDKYGWGAAAKITPTVLLLTGVGFFSLLLFGAPLAPTLAKFGMTPLLAAVYVGAMQNIFSKSAKYSLFDPCKEMAYIPLDEDTKVKGKAAIDVVCNPLGKSGGALIQQFMILTFGSLASSTPYLGGVLLVIVLAWLGAAKSLDGQFTQLRQEEDLEKEMERASLKIPVVSQNENGNGPLSSESSLNPAGGDSTNASSEPSSPRSL | Subcellular locations: Plastid, Chloroplast membrane |
TLP10_ORYSJ | Oryza sativa subsp. japonica | MAAVREPREEAAVGEGEGEEEGRWGGLLPELVEEVVRRVEASGGERWPARKDLVSCACVCRRWREAAAAVVRPLPESGRITFPSSLKQPGPKDFPIQCFVKRNKKKSMFYLYLGLLNGTMDKGKFLMAARRFRRGPHTEYVISLDADDLSQGSNAYVGKLRSDFWGTNFKIYDNQPPYDDAKTSSTRSSQRFGSTHRFGSRRICPQISAGNFNVGQISYKYNLLKSRGPRRMFCTMECPSTQETWENSLKTKSLRCTGTTVLRNKAPRWHEHLQCWCLNFHGRVTVASVKNFQLVATADPSHPDSVGDEETVILQFGKVDSNIFTMDYRQPLSAFQAFAICLSSFGTKLACE | Ubiquitous. |
TLP11_ORYSJ | Oryza sativa subsp. japonica | MSFRSVIQEVKGEIGAISRRGFRSRPGRVRRVAAAAEEPPDESSAAALVMRESCWTQLPPELLREVLARVEESEGWWPRRRDVVACAGVCRSWRGIVREIVRTPEASGNLTFPISLKQPGPRDAPMKCFIVRNRTTQTYYLYIGLTDALTDDGKFLLAARKCRRTTCTEYLISLDMNDISKRTDSYVGKLRSNFLGTKFTIYDAHPPYAGDVISKGQSARVIGSNHLSPRIPAGNYPVSHISYELNVLGSRGPRRMHCAMDSIPVSAIEQGGTAPTQTEFPLSYHESFTSIPFFKSKSVRANNSTASLLTQNGSKLVLKNKSPRWHEHLQCWCLNFHGRVTVASVKNFQLVASDESNPTNQEHDDVILQFGKVGKDMFTMDYRYPISAFQAFAICLSSFDTKIACE | Ubiquitous. |
TLP12_ORYSJ | Oryza sativa subsp. japonica | MSFRSIVRDVRDSFGSLSRRSFEVRISGLPGLSGHHRGKSLGSLSELRDRPVVVDQSRWVGLPPELLRDVMKRLEEGESNWPSRKDVVACAAVCRTWREICKDIVQSPEICGKLTFPVSLKQPGPRDGLIQCFIKRDKSKLTYYLYLCLSPAVLSENGKFLLAAKRNRRATSTEYIISVDSKNISRSSNGYVGKMRSNFLGTKFVVYDTQPPYNAGSLMSCQHGSRRISSRRVSPKLPTGSYPIAHVKYELNVLGTRGPRRMQCTMHSIPASAVDPEGVVPGQPEQLLPGPFEESFRSTNTSSRFSFMDRSLDFSSSRFSEISGSANQQGEDDIPEAKERPLVLRNKVPRWHEQLQCWCLNFRGRVTVASVKNFQLIAAASSESSQLEQQQQQQQQNHASSSSSASDHGKVILQFGKVGKDMFTMDYRYPLSAFQAFAICLTSFDTKLACE | Ubiquitous. |
TLP13_ORYSJ | Oryza sativa subsp. japonica | MSFRSIVRDVRDGFGSLSRRGFEVRILGHRRGKSHGAVHELHDPVPVIQSSCWASLPPELLRDIIERLEESEATWPSRKHVVACAGVCRTWREMCKEIVKNPELCGKITFPISLRQPGPRDGTMQCFIRRDKSTQTYYLYLSLGSAVLVDNGKFLLSAKRNWHATCTEYVISMNANNLSRSTNTNIGKLRSNFLGTKFVIYDTHTPYNATSDSQSGKTSRRFSNKGTAKHPCSTYSIANISYELNVFGTRGPRRMCCLMHSIPASSLEAGGTVPSQPDSILAHSLNESSFRSVSFSKSSVMDHSMHFSSAQFSDISIGDGPRIGGRVLSDDEECKETPLILQNKAPRWHEQLQCWCLNFRGRVTVASVKNFQLIAATQPAAGAPTPSQPVPPPPPEHDKVILQFGKVAKDMFTMDYHYPLSAFQAFAISLSSFDTKLACE | Ubiquitous. |
TLP14_ORYSJ | Oryza sativa subsp. japonica | MSFRSIVRDVRDGFGSLSRRGFEVRLVGHRRGRSHSAVHELRDGHAAAAAADVVQSSCWANLPPELLRDVIERLEASEAAWPSRKNVVACAAVCRTWRDMCREIVKNPEFCGKITFPVSLKQPGPRNGAIQCFIKRDKSTQTYNLYLCLSSAVLVESGKFLLSAKRYSRATCTEYTIFMSADNTSRSSNMYIGKLRSNLLGTKFVIYDTQPPCNTANVSQSGKTSRRFYSRKVSPKNPSSTYSIAQVSYELNVLGTRGPRRMNCVMHSIPASSLEAGGTVPCQPDSVLARSLDESFGSISFSKSSIMDRSIRFSSSRYSDISVGGPMVGGQALGDSDESKERPLILRNKAPRWHEQLQCWCLNFKGRVTVASVKNFQLVAATQPAAGAPTPSQPAPPPPPDHDKVILQFGKVAKDMFTMDYRYPLSAFQAFAICLSSFDTKLACE | Ubiquitous. |
TM1R_SOLLC | Solanum lycopersicum | MATAQSNSPRVFCIGTADTKFDELRFLSEHVRSSLNSFSNKSSFKVGVTVVDVSTSWKETNSCADFDFVPSKDVLSCHTLGEETMGTFADIRGLAIAIMSKALETFLSIANDEQNLAGVIGLGGSGGTSLLSSAFRSLPIGIPKVIISTVASGQTESYIGTSDLVLFPSVVDICGINNVSKVVLSNAGAAFAGMVIGRLESSKEHSITNGKFTVGVTMFGVTTPCVNAVKERLVKEGYETLVFHATGVGGRAMEDLVRGGFIQGVLDITTTEVADYVVGGVMACDSSRFDAILEKKIPLVLSVGALDMVNFGPKTTIPPEFQQRKIHEHNEQVSLMRTTVGENKKFAAFIAEKLNKASSSVCVCLPEKGVSALDAPGKDFYDPEATSCLTRELQMLLENNERCQVKVLPYHINDAEFANALVDSFLEISPKSRHVECQPAESKSIQDIQNDNAVLEKYPSCNGKNFSRLNDFPNAKPETLQKRTVILQKLKDQISKGKPIIGAGAGTGISAKFEEAGGVDLIVLYNSGRFRMAGRGSLAGLLPFADANAIVLEMANEVLPVVKEVAVLAGVCATDPFRRMDNFLKQLESVGFCGVQNFPTVGLFDGNFRQNLEETGMGYGLEVEMIAAAHRMGLLTTPYAFCPDEAVAMAEAGADIIVAHMGLTTSGSIGAKTAVSLEESVTCVQAIADATHRIYPDAIVLCHGGPISSPEEAAYVLKRTTGVHGFYGASSMERLPVEQAITATVQQYKSISME | Inhibitor of viral RNA replication which confers resistance to some tobamoviruses including tomato mosaic virus (ToMV) (e.g. isolate L), tobacco mosaic virus (TMV), tobacco mild green mosaic virus (TMGMV) and pepper mild mottle virus (PMMoV), but not to resistance-breaking isolates of ToMV (e.g. LT1, SL-1 and ToMV1-2) and tomato brown rugose fruit virus (ToBRFV) ( ). Prevents tobamoviruses RNA replication by affecting the association of tobamoviruses replication proteins (large and small subunits) with host membrane-associated proteins (e.g. TOM1, TOM2A and ARL8), thus inhibiting the replication complex formation on the membranes and avoiding viral negative-strand RNA synthesis ( , ). Inhibits triphosphatase activity of ToMV replication proteins . |
TM1S_SOLLC | Solanum lycopersicum | MATAQSNSPRVFCIGTADTKFDELRFLSEHVRSSLNSFSNKSSFKVGVTVVDVSTSRKETNSCADFDFVPSKDVLSCYARGEGTVGRFPDIRGQAIAIMNKALETFLSKANGEQNLAGVIGLGGSGGTSLLSSAFRSLPIGIPKVIISTVASGQTESYIGTSDLVLFPSVVDICGINNVSKVVLSNAGAAFAGMVIGRLESSKEHSITNGKFTVGVTMFGVTTPCVNAVKERLVKEGYETLVFHATGVGGRAMEDLVRGGFIQGVLDITTTEVADYVVGGVMACDSSRFDAILEKKIPLVLSVGALDMVNFGPKTTIPPEFQQRKIHQHNEQVSLMHTTVGENKKFAAFIAEKLNKASSSVCVCLPEKGVSALDAPGKDFYDPEATSCLTHELQMLLENNERCQVKVYPYHINDVEFANALVDSFLEMSPKSGHVECQTAESKSIQGIQNVNAVLEKYPSCNGKNFSRLNDFPNAKPETLQKRIVILQKLKDQISKGKPIIGAGAGTGISAKFEEAGGVDLIVLYNSGRFRMAGRGSLAGLLPFADANAIVLEMANEVLPVVKEVAVLAGVCATDPFRRMDNFLKQLESVGFCGVQNFPTVGLFDGNFRQNLEETGMGYGLEVEMIATAHRMGLLTTPYAFCPDEAVAMAEAGADIIVAHMGLTTSGSIGAKTAVSLEESVTCVQAIADATHRINPDAIVLCHGGPISSPEEAAYVLKRTTGVHGFYGASSMERLPVEQAITATVQQYKSISME | Inhibitor of viral RNA replication which confers resistance to some tobamoviruses including tobacco mild green mosaic virus (TMGMV) and pepper mild mottle virus (PMMoV), but not to tomato mosaic virus (ToMV strains L, ToMV0 and ToMV1-2) and tobacco mosaic virus (TMV) ( ). Prevents tobamoviruses RNA replication by affecting the association of tobamoviruses replication proteins (large and small subunits) with host membrane-associated proteins (e.g. TOM1, TOM2A and ARL8), thus inhibiting the replication complex formation on the membranes and avoiding viral negative-strand RNA synthesis . |
TOM7A_SOLTU | Solanum tuberosum | MLKPKGKNTKKAAAADEDDGAVAVVGKFVKEWGTWTAKKAKVITHYGFIPLVIIIGMNSEPKPSLSQLLSPV | Seems to act as a modulator of the dynamics of the mitochondrial protein transport machinery. Seems to promote the dissociation of subunits of the outer membrane translocase (By similarity).
Subcellular locations: Mitochondrion outer membrane |
TOM7B_SOLTU | Solanum tuberosum | AKGKNTKKFAAVVDEEGGAVTAXYXF | Seems to act as a modulator of the dynamics of the mitochondrial protein transport machinery. Seems to promote the dissociation of subunits of the outer membrane translocase (By similarity).
Subcellular locations: Mitochondrion outer membrane |
TPIC_SECCE | Secale cereale | MAARRPSPPPASPPPPRPRSTTTTRTTSSASAAPAAAQRLVAMAGSGKFFVGGNWKCNGTKESISKLVSDLNAATLESDVDVVVAPPFIYIDQVKSSLTDRIEVSAQNTWIGKGGAFTGEISAEQLVDIGCQWVILGHSERRHVIGEDDEFIGKKAAYALSQNLKVMACIGELLEEREAGKTFDVCFKQMKAFADNITDWTNVVIAYEPVWAIGTGKVASPEQAQEVHAAVRDWLKTNVSADVASTVRIIYGGSVNAANCAELAKKEDIDGFLVGGASLKGPDFATICNSVTSKKVTA | Subcellular locations: Plastid, Chloroplast |
TPIC_SPIOL | Spinacia oleracea | MAVVSTSLASQITNPNSAVSTQFSGLRRSFLKLENSVSTQSSFFQNVDSHLRLSSSSRRCPRGVVAMAGSGKFFVGGNWKCNGTKESITKLVSDLNSATLEADVDVVVAPPFVYIDQVKSSLTGRVEISAQNCWIGKGGAFTGEISVEQLKDLGCQWVILGHSERRHVIGEQNEFIGKKAAYALNQGVGVIACIGELLEEREAGKTFDVCYQQLKAFADALPSWDNVVVAYEPVWAIGTGKVASPDQAQEVHVAVRDWLKKNVSEEVASKTRIIYGGSVNGGNCAELAKQEDIDGFLVGGASLKGPEFATIVNSVTAKKVAA | Subcellular locations: Plastid, Chloroplast |
TPIS_MAIZE | Zea mays | MGRKFFVGGNWKCNGTTDQVEKIVKTLNEGQVPPSDVVEVVVSPPYVFLPVVKSQLRQEFHVAAQNCWVKKGGAFTGEVSAEMLVNLGVPWVILGHSERRALLGESNEFVGDKVAYALSQGLKVIACVGETLEQREAGSTMDVVAAQTKAIAEKIKDWSNVVVAYEPVWAIGTGKVATPAQAQEVHASLRDWLKTNASPEVAESTRIIYGGSVTAANCKELAAQPDVDGFLVGGASLKPEFIDIINAATVKSA | Subcellular locations: Cytoplasm |
TPS11_MAIZE | Zea mays | MAAPTLTTDGPRLGQQEMKKMSPSFHPTLWGDFFLSYEAPTEAQEAEMRQRAEVLREEVRNMIKGSHDVPEIVDLIITLQRLNLDYHYEDEINEKLAVVYNSNYDGGNLDLVSRRFYLLRKCGYHVSSDVFLNFKDQYGNFIEVDTRSLLSLYNAAYLRIHGETVLDEAISFTTRCLQDRLEHLESPIAEEVSSALDTPLFRRVGTLEMKDYIPIYEKDAKQNKSILEFAKLNFNLLQLLYSSELKECTTWWKELRVESNLSFVRDRIVEVYFWMSGGCYDPQYSHSRIILTKIVAFITILDDTLDSHANSYESMQLAEAVERWDESAVSLLPEYMKDFYMYLLKTFSSFENELGPDKSYRVFYLKEAVKELVREYTKEIKWRDEDYVPKTLKEHLKVSLISIGGTLVLCSAFVGMGDVVTKKIMEWVMSDAELVKSFGIFVRLSNDIVSTKREQREKHCVSTVQCYMKQHELTMDEACEQIKELTEDSWKFMIEQGLALKEYPIIVPRTVLEFARTVDYMYKEADKYTVSHTIKDMLTSLYVKPVLM | Involved in the biosynthesis of the bicyclic sesquiterpene (S)-beta-macrocarpene. Can use both geranyl diphosphate and farnesyl diphosphate as substrate, but not geranylgeranyl diphosphate. Produces mainly (S)-beta-macrocarpene, but also smaller amounts of beta-bisabolene and (E)-beta-farnesene when used with farnesyl diphosphate as substrate. In the presence of geranyl diphosphate, produces the acyclic monoterpenes beta-myrcene and linalool along with minor amounts of the cyclic compounds limonene, alpha-thujene, sabinene and alpha-terpinolene. May be involved in plant defense.
Subcellular locations: Cytoplasm
Expressed in roots. Not detected in leaves, unless damaged by herbivory or infected by fungi. |